NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|608788355|ref|NP_001243426|]
View 

CYP3A7-CYP3A51P protein [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
67-492 0e+00

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: 858.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  67 KYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMV 146
Cdd:cd20650    1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 147 PIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVF 226
Cdd:cd20650   81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 227 PFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFAG 306
Cdd:cd20650  161 PFLTPILEKLNISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 307 YETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGM 386
Cdd:cd20650  241 YETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 387 FIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20650  321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                        410       420
                 ....*....|....*....|....*.
gi 608788355 467 PCKETQIPLKLRFGGLLLTEKPIVLK 492
Cdd:cd20650  401 PCKETQIPLKLSLQGLLQPEKPIVLK 426
 
Name Accession Description Interval E-value
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
67-492 0e+00

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: 858.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  67 KYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMV 146
Cdd:cd20650    1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 147 PIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVF 226
Cdd:cd20650   81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 227 PFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFAG 306
Cdd:cd20650  161 PFLTPILEKLNISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 307 YETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGM 386
Cdd:cd20650  241 YETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 387 FIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20650  321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                        410       420
                 ....*....|....*....|....*.
gi 608788355 467 PCKETQIPLKLRFGGLLLTEKPIVLK 492
Cdd:cd20650  401 PCKETQIPLKLSLQGLLQPEKPIVLK 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
39-492 2.06e-146

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: 428.62  E-value: 2.06e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355   39 PGPTPLPFLGNALSFRKG--YWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFG----PVG 112
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfatsRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  113 FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVS 192
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  193 IDSLNNPQDP-FVENTKKLL------RFNPLDPFVLsikVFPFLTPILEALNITVfpRKVISFLTKSVKQIKEgRLKETQ 265
Cdd:pfam00067 162 FGSLEDPKFLeLVKAVQELSsllsspSPQLLDLFPI---LKYFPGPHGRKLKRAR--KKIKDLLDKLIEERRE-TLDSAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  266 KHRVDFLQLMIDSQNSKDsetHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP 345
Cdd:pfam00067 236 KSPRDFLDALLLAKEEED---GSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  346 TYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNK 424
Cdd:pfam00067 313 TYDDLQNMPYLDAVIKETLRLHPVVpLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 608788355  425 DNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKPIVLK 492
Cdd:pfam00067 393 KFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLK 460
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-463 4.47e-63

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: 211.68  E-value: 4.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVK-ECYSV-FTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQygdvL 156
Cdd:COG2124   42 GGAWLVTRYEDVREVLRDpRTFSSdGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIRE----I 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 157 VRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnpQDPFVENTKKLLR-FNPLDPfvlsikvfPFLTPILEA 235
Cdd:COG2124  118 ADELLDRLAARGPVDLVEEFARPLPVIVICELLGVPEED----RDRLRRWSDALLDaLGPLPP--------ERRRRARRA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 236 LnitvfpRKVISFLTKsvkQIKEGRlketQKHRVDFLQLMIDSQnskdsETHKALSDLELMAQSIIFIFAGYETTSSVLS 315
Cdd:COG2124  186 R------AELDAYLRE---LIAERR----AEPGDDLLSALLAAR-----DDGERLSDEELRDELLLLLLAGHETTANALA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 316 FIIYELATHPDVQQKVQKEidtvlpnkapptydtvlqLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVM 395
Cdd:COG2124  248 WALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVL 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 608788355 396 IPSYVLHHDPKYWTEPEKFLPERfskknkdniDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:COG2124  310 LSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRF 368
PLN02290 PLN02290
cytokinin trans-hydroxylase
23-465 1.26e-47

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 173.08  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  23 YLYGTRTHGLFKKLGIPGPTPLPFLGNAL---SFRKGYWTFDMECY----------------KKYRKVWGIYDCQQPMLA 83
Cdd:PLN02290  29 FLTPRRIKKIMERQGVRGPKPRPLTGNILdvsALVSQSTSKDMDSIhhdivgrllphyvawsKQYGKRFIYWNGTEPRLC 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVLVKecYSVFTNR---RPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNL 160
Cdd:PLN02290 109 LTETELIKELLTK--YNTVTGKswlQQQGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 161 RREAETGKP-VTLKHVFGAYSMDVITSTSFGVSIDS-------LNNPQDPFVENTKKLL----RFNPlDPFVLSIKvfpf 228
Cdd:PLN02290 187 QKAVESGQTeVEIGEYMTRLTADIISRTEFDSSYEKgkqifhlLTVLQRLCAQATRHLCfpgsRFFP-SKYNREIK---- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 229 ltpileALNITVfPRKVISFLTKSVKQIKEGRlkeTQKHRVDFLQLMIDSQNSKDSETHKAlsDLEL-MAQSIIFIFAGY 307
Cdd:PLN02290 262 ------SLKGEV-ERLLMEIIQSRRDCVEIGR---SSSYGDDLLGMLLNEMEKKRSNGFNL--NLQLiMDECKTFFFAGH 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 308 ETTSSVLSFIIYELATHPDVQQKVQKEIDTVLpNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMF 387
Cdd:PLN02290 330 ETTALLLTWTLMLLASNPTWQDKVRAEVAEVC-GGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH 408
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 388 IPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSKKNKDNIDPYIytPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:PLN02290 409 IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFI--PFAAGPRNCIGQAFAMMEAKIILAMLISKFSF 485
 
Name Accession Description Interval E-value
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
67-492 0e+00

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: 858.25  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  67 KYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMV 146
Cdd:cd20650    1 KYGKVWGIYDGRQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRIRSLLSPTFTSGKLKEMF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 147 PIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVF 226
Cdd:cd20650   81 PIIAQYGDVLVKNLRKEAEKGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLKFDFLDPLFLSITVF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 227 PFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFAG 306
Cdd:cd20650  161 PFLTPILEKLNISVFPKDVTNFFYKSVKKIKESRLDSTQKHRVDFLQLMIDSQNSKETESHKALSDLEILAQSIIFIFAG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 307 YETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGM 386
Cdd:cd20650  241 YETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEINGV 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 387 FIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20650  321 FIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDNIDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK 400
                        410       420
                 ....*....|....*....|....*.
gi 608788355 467 PCKETQIPLKLRFGGLLLTEKPIVLK 492
Cdd:cd20650  401 PCKETQIPLKLSLQGLLQPEKPIVLK 426
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
67-490 0e+00

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: 589.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  67 KYRKVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNRRPFGPVG-FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEM 145
Cdd:cd11055    1 KYGKVFGLYFGTIPVIVVSDPEMIKEILVKE-FSNFTNRPLFILLDePFDSSLLFLKGERWKRLRTTLSPTFSSGKLKLM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 146 VPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIkv 225
Cdd:cd11055   80 VPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIRLFLLLL-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 226 FPFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFA 305
Cdd:cd11055  158 LFPLRLFLFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNKSSRRKDLLQLMLDAQDSDEDVSKKKLTDDEIVAQSFIFLLA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 306 GYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEING 385
Cdd:cd11055  238 GYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTING 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 386 MFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd11055  318 VFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRF 397
                        410       420
                 ....*....|....*....|....*
gi 608788355 466 KPCKETQIPLKLRFGGLLLTEKPIV 490
Cdd:cd11055  398 VPCKETEIPLKLVGGATLSPKNGIY 422
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
70-487 2.98e-157

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: 455.07  E-value: 2.98e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  70 KVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNRRPFGPVGF--MKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVP 147
Cdd:cd11056    4 PFVGIYLFRRPALLVRDPELIKQILVKD-FAHFHDRGLYSDEKDdpLSANLFSLDGEKWKELRQKLTPAFTSGKLKNMFP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 148 IIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFvlsIKVFP 227
Cdd:cd11056   83 LMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFGLDANSLNDPENEFREMGRRLFEPSRLRGL---KFMLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 228 FLTP-ILEALNITVFPRKVISFLTKSVKQIKEGRlKETQKHRVDFLQLMIDSQNSK---DSETHKALSDLELMAQSIIFI 303
Cdd:cd11056  160 FFFPkLARLLRLKFFPKEVEDFFRKLVRDTIEYR-EKNNIVRNDFIDLLLELKKKGkieDDKSEKELTDEELAAQAFVFF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 304 FAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLP-NKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVE 382
Cdd:cd11056  239 LAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEkHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYT 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 383 ING--MFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVL 460
Cdd:cd11056  319 LPGtdVVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFSPENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLL 398
                        410       420
                 ....*....|....*....|....*..
gi 608788355 461 QNFSFKPCKETQIPLKLRFGGLLLTEK 487
Cdd:cd11056  399 SNFRVEPSSKTKIPLKLSPKSFVLSPK 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
39-492 2.06e-146

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: 428.62  E-value: 2.06e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355   39 PGPTPLPFLGNALSFRKG--YWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRPFG----PVG 112
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKgnLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWfatsRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  113 FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVS 192
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  193 IDSLNNPQDP-FVENTKKLL------RFNPLDPFVLsikVFPFLTPILEALNITVfpRKVISFLTKSVKQIKEgRLKETQ 265
Cdd:pfam00067 162 FGSLEDPKFLeLVKAVQELSsllsspSPQLLDLFPI---LKYFPGPHGRKLKRAR--KKIKDLLDKLIEERRE-TLDSAK 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  266 KHRVDFLQLMIDSQNSKDsetHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP 345
Cdd:pfam00067 236 KSPRDFLDALLLAKEEED---GSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSP 312
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  346 TYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNK 424
Cdd:pfam00067 313 TYDDLQNMPYLDAVIKETLRLHPVVpLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENG 392
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 608788355  425 DNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKPIVLK 492
Cdd:pfam00067 393 KFRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLK 460
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
67-478 1.04e-130

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: 388.43  E-value: 1.04e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  67 KYRKVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNRRPFGPVGF-MKNAISIAEDEEWKRIRSLLSPTFTSGKLKEM 145
Cdd:cd20649    1 KYGPICGYYIGRRMFVVIAEPDMIKQVLVKD-FNNFTNRMKANLITKpMSDSLLCLRDERWKRVRSILTPAFSAAKMKEM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 146 VPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKV 225
Cdd:cd20649   80 VPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQKNPDDPFVKNCKRFFEFSFFRPILILFLA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 226 FPF-LTPILEALnitvfPRK----VISFLTKSVKQIKEGRLKET-QKHRVDFLQLMIDSQNSK--------------DSE 285
Cdd:cd20649  160 FPFiMIPLARIL-----PNKsrdeLNSFFTQCIRNMIAFRDQQSpEERRRDFLQLMLDARTSAkflsvehfdivndaDES 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 286 TH------------------KALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTY 347
Cdd:cd20649  235 AYdghpnspaneqtkpskqkRMLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDY 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 348 DTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNI 427
Cdd:cd20649  315 ANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRR 394
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 608788355 428 DPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLR 478
Cdd:cd20649  395 HPFVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETEIPLQLK 445
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
79-489 3.72e-101

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: 311.38  E-value: 3.72e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVL--VKEC-----YSVFtnrRPFgpvgfMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQ 151
Cdd:cd20628   11 KPYVVVTNPEDIEVILssSKLItksflYDFL---KPW-----LGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 152 YGDVLVRNLRREAEtGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLR------FNPLdpfvLSIKV 225
Cdd:cd20628   83 NSKILVEKLKKKAG-GGEFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEiilkriFSPW----LRFDF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 226 FPFLTPI----LEALN-ITVFPRKVIsflTKSVKQIKEGRLKET------QKHRVDFLQLMIDSQnskdsETHKALSDLE 294
Cdd:cd20628  158 IFRLTSLgkeqRKALKvLHDFTNKVI---KERREELKAEKRNSEeddefgKKKRKAFLDLLLEAH-----EDGGPLTDED 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 295 LMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL-PNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRL 373
Cdd:cd20628  230 IREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFgDDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFI 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 374 ERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMK 453
Cdd:cd20628  310 GRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPRNCIGQKFAMLEMK 389
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 608788355 454 LALVRVLQNFSFKPCKETQiPLKLRFGGLLLTEKPI 489
Cdd:cd20628  390 TLLAKILRNFRVLPVPPGE-DLKLIAEIVLRSKNGI 424
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
79-466 1.74e-91

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: 286.72  E-value: 1.74e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKE-------CYSVFTNrrPFGpVGFMKNAI-SIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIA 150
Cdd:cd20613   22 RPIVVVSDPEAVKEVLITLnlpkpprVYSRLAF--LFG-ERFLGNGLvTEVDHEKWKKRRAILNPAFHRKYLKNLMDEFN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 151 QYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLR------FNPLdpFVLSIK 224
Cdd:cd20613   99 ESADLLVEKLSKKADGKTEVNMLDEFNRVTLDVIAKVAFGMDLNSIEDPDSPFPKAISLVLEgiqesfRNPL--LKYNPS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 225 VFPFLTPILEALN-ITVFPRKVIsflTKSVKQIKEGrlKETQKhrvDFLQLMIdsQNSKDSETHkalsDLELMAQSII-F 302
Cdd:cd20613  177 KRKYRREVREAIKfLRETGRECI---EERLEALKRG--EEVPN---DILTHIL--KASEEEPDF----DMEELLDDFVtF 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 303 IFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVE 382
Cdd:cd20613  243 FIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIE 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 383 INGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQN 462
Cdd:cd20613  323 LGGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPFSLGPRSCIGQQFAQIEAKVILAKLLQN 402

                 ....
gi 608788355 463 FSFK 466
Cdd:cd20613  403 FKFE 406
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
79-485 8.70e-91

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: 283.64  E-value: 8.70e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKECY-SVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLV 157
Cdd:cd00302   11 GPVVVVSDPELVREVLRDPRDfSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIREIARELL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 158 RNLRREAETGKPVTlkHVFGAYSMDVITSTSFGvsiDSLNNPQDPFVENTKKLLRFnpLDPFVLSIKVFPFLTPILEALn 237
Cdd:cd00302   91 DRLAAGGEVGDDVA--DLAQPLALDVIARLLGG---PDLGEDLEELAELLEALLKL--LGPRLLRPLPSPRLRRLRRAR- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 238 itvfpRKVISFLTKSVKQikegRLKETQKHRVDFLQLmidsqnskDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFI 317
Cdd:cd00302  163 -----ARLRDYLEELIAR----RRAEPADDLDLLLLA--------DADDGGGLSDEEIVAELLTLLLAGHETTASLLAWA 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 318 IYELATHPDVQQKVQKEIDTVLPNkapPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIP 397
Cdd:cd00302  226 LYLLARHPEVQERLRAEIDAVLGD---GTPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLS 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 398 SYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIytPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKL 477
Cdd:cd00302  303 LYAAHRDPEVFPDPDEFDPERFLPEREEPRYAHL--PFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEELEWRP 380

                 ....*...
gi 608788355 478 RFGGLLLT 485
Cdd:cd00302  381 SLGTLGPA 388
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
80-478 1.89e-87

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: 276.46  E-value: 1.89e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKECYS------VFTNRRPFGPVGFMknaisIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYG 153
Cdd:cd11069   14 ERLLVTDPKALKHILVTNSYDfekppaFRRLLRRILGDGLL-----AAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKA 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 154 DVLVRNLRREAETGKPVTLK----HVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLlrFNPLDPFVLSIKVFPFL 229
Cdd:cd11069   89 EELVDKLEEEIEESGDESISidvlEWLSRATLDIIGLAGFGYDFDSLENPDNELAEAYRRL--FEPTLLGSLLFILLLFL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 230 TPILE-----ALNITVfpRKVISFLTKSVKQI----KEGRLKETQKHRVDFLQLMIDSqnsKDSETHKALSDLELMAQSI 300
Cdd:cd11069  167 PRWLVrilpwKANREI--RRAKDVLRRLAREIirekKAALLEGKDDSGKDILSILLRA---NDFADDERLSDEELIDQIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNK--APPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCK 378
Cdd:cd11069  242 TFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDPpdGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREAT 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 379 KDVEINGMFIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERF---SKKNKDNI--DPYIYTPFGSGPRNCIGMRFALVNM 452
Cdd:cd11069  322 KDTVIKGVPIPKGTVVLIPPAAINRSPEIWGPdAEEFNPERWlepDGAASPGGagSNYALLTFLHGPRSCIGKKFALAEM 401
                        410       420
                 ....*....|....*....|....*.
gi 608788355 453 KLALVRVLQNFSFKPCKETQIPLKLR 478
Cdd:cd11069  402 KVLLAALVSRFEFELDPDAEVERPIG 427
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
79-494 8.36e-82

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: 261.34  E-value: 8.36e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKecysvfTNRRPFGPVGFMK----NAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGD 154
Cdd:cd20659   12 RPILVLNHPDTIKAVLKT------SEPKDRDSYRFLKpwlgDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECTD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSID-SLNNPQDPFVENTKKLLR------FNPLdpfvLSIKVFP 227
Cdd:cd20659   86 ILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNcQQTGKNHPYVAAVHELSRlvmerfLNPL----LHFDWIY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 228 FLTP----ILEALNIT-VFPRKVISFLTKSVKQIKEGRLKETQKhrVDFLQLMIDsqnSKDsETHKALSDLELMAQSIIF 302
Cdd:cd20659  162 YLTPegrrFKKACDYVhKFAEEIIKKRRKELEDNKDEALSKRKY--LDFLDILLT---ARD-EDGKGLTDEEIRDEVDTF 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 303 IFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVE 382
Cdd:cd20659  236 LFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPIT 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 383 INGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQN 462
Cdd:cd20659  316 IDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKKRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRR 395
                        410       420       430
                 ....*....|....*....|....*....|..
gi 608788355 463 FSFKPCKETQIPLKLrfggllltekPIVLKAE 494
Cdd:cd20659  396 FELSVDPNHPVEPKP----------GLVLRSK 417
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
79-467 5.39e-80

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: 255.97  E-value: 5.39e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVkecysvfTNRRPFGPVGFMK-------NAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQ 151
Cdd:cd20620   11 RRVYLVTHPDHIQHVLV-------TNARNYVKGGVYErlklllgNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 152 YGDVLVRNLRrEAETGKPVTLKHVFGAYSMDVITSTSFGVS----IDSLNNPQDPFVENTKKLLRfNPLDPFvlsikvFP 227
Cdd:cd20620   84 ATAALLDRWE-AGARRGPVDVHAEMMRLTLRIVAKTLFGTDvegeADEIGDALDVALEYAARRML-SPFLLP------LW 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 228 FLTPILEALnitvfpRKVISFLTKSVKQIKEGRLKETQKHrVDFLQLMIDSQnskDSETHKALSDLELMAQSIIFIFAGY 307
Cdd:cd20620  156 LPTPANRRF------RRARRRLDEVIYRLIAERRAAPADG-GDLLSMLLAAR---DEETGEPMSDQQLRDEVMTLFLAGH 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 308 ETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKaPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMF 387
Cdd:cd20620  226 ETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGR-PPTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYR 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 388 IPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd20620  305 IPAGSTVLISPYVTHRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRL 384
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
80-479 1.01e-79

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: 255.99  E-value: 1.01e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVK-ECYSvftnrRPFGPVGF-MKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLV 157
Cdd:cd11057   12 PFVITSDPEIVQVVLNSpHCLN-----KSFFYDFFrLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 158 RNLRREAeTGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLR------FNPLdpfvLSIKVFPFLTP 231
Cdd:cd11057   87 QRLDTYV-GGGEFDILPDLSRCTLEMICQTTLGSDVNDESDGNEEYLESYERLFEliakrvLNPW----LHPEFIYRLTG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 232 -----ILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFlQLMIDsQNSKDSETHKALSDLELMAQSIIFIFAG 306
Cdd:cd11057  162 dykeeQKARKILRAFSEKIIEKKLQEVELESNLDSEEDEENGRKP-QIFID-QLLELARNGEEFTDEEIMDEIDTMIFAG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 307 YETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNK-APPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEI-N 384
Cdd:cd11057  240 NDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDDgQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLsN 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 385 GMFIPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd11057  320 GVVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNY 399
                        410
                 ....*....|....*..
gi 608788355 464 SFKpckeTQIPLK-LRF 479
Cdd:cd11057  400 RLK----TSLRLEdLRF 412
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
70-488 2.86e-79

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: 254.44  E-value: 2.86e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  70 KVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNR--RPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFT-SGKLKEMV 146
Cdd:cd20617    2 GIFTLWLGDVPTVVLSDPEIIKEAFVKN-GDNFSDRplLPSFEIISGGKGILFSNGDYWKELRRFALSSLTkTKLKKKME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 147 PIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQ-----DPFVENTKKLLRFNPLDPFVL 221
Cdd:cd20617   81 ELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEflklvKPIEEIFKELGSGNPSDFIPI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 222 SIKVFPFLTPILEALNitvfpRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSEThkalsDLELMAQSII 301
Cdd:cd20617  161 LLPFYFLYLKKLKKSY-----DKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFD-----DDSIISTCLD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 302 FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKD 380
Cdd:cd20617  231 LFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILpLGLPRVTTED 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 381 VEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF-SKKNKDNIDPYIytPFGSGPRNCIGMRFALVNMKLALVRV 459
Cdd:cd20617  311 TEIGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNKLSEQFI--PFGIGKRNCVGENLARDELFLFFANL 388
                        410       420
                 ....*....|....*....|....*....
gi 608788355 460 LQNFSFKPCKETQIPLKLrFGGLLLTEKP 488
Cdd:cd20617  389 LLNFKFKSSDGLPIDEKE-VFGLTLKPKP 416
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
79-489 8.38e-77

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: 248.21  E-value: 8.38e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKEcySVFTNRRPFGPVGFMKN------AISIAEDEEWKRIRSLLSPTFTSGK-LKEMVPIIAQ 151
Cdd:cd11054   15 RDIVHLFDPDDIEKVFRNE--GKYPIRPSLEPLEKYRKkrgkplGLLNSNGEEWHRLRSAVQKPLLRPKsVASYLPAINE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 152 YGDVLVRNLR--REAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDP----FVENTKKLLR-FNPLDPFVLSIK 224
Cdd:cd11054   93 VADDFVERIRrlRDEDGEEVPDLEDELYKWSLESIGTVLFGKRLGCLDDNPDSdaqkLIEAVKDIFEsSAKLMFGPPLWK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 225 VFPflTPI---LEALNITVFpRKVISFLTKSVKQIKEGRLKEtqKHRVDFL-QLMIDSQNSKDsethkalsdlELMAQSI 300
Cdd:cd11054  173 YFP--TPAwkkFVKAWDTIF-DIASKYVDEALEELKKKDEED--EEEDSLLeYLLSKPGLSKK----------EIVTMAL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKD 380
Cdd:cd11054  238 DLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKD 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 381 VEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF--SKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVR 458
Cdd:cd11054  318 IVLSGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrDDSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAK 397
                        410       420       430
                 ....*....|....*....|....*....|.
gi 608788355 459 VLQNFSFKPCKEtqiPLKLRFGGLLLTEKPI 489
Cdd:cd11054  398 LLQNFKVEYHHE---ELKVKTRLILVPDKPL 425
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
104-470 2.09e-76

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: 247.11  E-value: 2.09e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 104 NRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDV 183
Cdd:cd11058   36 DPRFYPPAPNGPPSISTADDEDHARLRRLLAHAFSEKALREQEPIIQRYVDLLVSRLRERAGSGTPVDMVKWFNFTTFDI 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 184 ITSTSFGVSIDSL-NNPQDPFVENTKKLLRFNPldpFVLSIKVFPFLTPILEALnitvFPRKVISFLTKSVKQIKEG--- 259
Cdd:cd11058  116 IGDLAFGESFGCLeNGEYHPWVALIFDSIKALT---IIQALRRYPWLLRLLRLL----IPKSLRKKRKEHFQYTREKvdr 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 260 RLkETQKHRVDFLQLMIdsqnsKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL 339
Cdd:cd11058  189 RL-AKGTDRPDFMSYIL-----RNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAF 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 340 PNKAPPTYDTVLQLEYLDMVVNETLRLF-PVAMRLERVCKKD-VEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPE 417
Cdd:cd11058  263 SSEDDITLDSLAQLPYLNAVIQEALRLYpPVPAGLPRVVPAGgATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPE 342
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 608788355 418 R--------FSKKNKDnidpyIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKE 470
Cdd:cd11058  343 RwlgdprfeFDNDKKE-----AFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPE 398
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
82-466 2.08e-72

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: 236.74  E-value: 2.08e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  82 LAITDPDMIKTVL--VKEC-----YSVFTNRRPfgpvgfmkNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGD 154
Cdd:cd11061   11 LSINDPDALKDIYghGSNClkgpfYDALSPSAS--------LTFTTRDKAEHARRRRVWSHAFSDKALRGYEPRILSHVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNLRREA--ETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVEntkKLLRFNPLDPFVLSIkvFPFLTPI 232
Cdd:cd11061   83 QLCEQLDDRAgkPVSWPVDMSDWFNYLSFDVMGDLAFGKSFGMLESGKDRYIL---DLLEKSMVRLGVLGH--APWLRPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 233 LeaLNITVFP---RKVISFLTKSVKQIKEgRLKETQKHRVDFLQLMIdsqNSKDSETHKALSDLELMAQSIIFIFAGYET 309
Cdd:cd11061  158 L--LDLPLFPgatKARKRFLDFVRAQLKE-RLKAEEEKRPDIFSYLL---EAKDPETGEGLDLEELVGEARLLIVAGSDT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 310 TSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKA-PPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVCKKD-VEINGM 386
Cdd:cd11061  232 TATALSAIFYYLARNPEAYEKLRAELDSTFPSDDeIRLGPKLKSLPYLRACIDEALRLSPpVPSGLPRETPPGgLTIDGE 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 387 FIPKGVVVMIPSYVLHHDPKYWTEPEKFLPER-FSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd11061  312 YIPGGTTVSVPIYSIHRDERYFPDPFEFIPERwLSRPEELVRARSAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDF 391

                 .
gi 608788355 466 K 466
Cdd:cd11061  392 R 392
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
84-466 8.54e-69

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: 227.52  E-value: 8.54e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVlvkecYSVFTNRR-----PFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVR 158
Cdd:cd11062   13 ISDPDFYDEI-----YAGGSRRRkdppyFYGAFGAPGSTFSTVDHDLHRLRRKALSPFFSKRSILRLEPLIQEKVDKLVS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 159 NLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQdpFVENTKKLLRFnpLDPFVLSIKVFPFLTPILEALNI 238
Cdd:cd11062   88 RLREAKGTGEPVNLDDAFRALTADVITEYAFGRSYGYLDEPD--FGPEFLDALRA--LAEMIHLLRHFPWLLKLLRSLPE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 239 TVFPR------KVISFLTKSVKQIKEGRLKETQKH---RVDFLQLMIDSQNSKDSEthkaLSDLELMAQSIIFIFAGYET 309
Cdd:cd11062  164 SLLKRlnpglaVFLDFQESIAKQVDEVLRQVSAGDppsIVTSLFHALLNSDLPPSE----KTLERLADEAQTLIGAGTET 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 310 TSSVLSFIIYELATHPDVQQKVQKEIDTVLPNK-APPTYDTVLQLEYLDMVVNETLRL-FPVAMRLERVC-KKDVEINGM 386
Cdd:cd11062  240 TARTLSVATFHLLSNPEILERLREELKTAMPDPdSPPSLAELEKLPYLTAVIKEGLRLsYGVPTRLPRVVpDEGLYYKGW 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 387 FIPKGVVVMIPSYVLHHDPKYWTEPEKFLPER-FSKKNKDNIDPYiYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd11062  320 VIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERwLGAAEKGKLDRY-LVPFSKGSRSCLGINLAYAELYLALAALFRRFDL 398

                 .
gi 608788355 466 K 466
Cdd:cd11062  399 E 399
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
79-483 5.35e-68

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: 225.21  E-value: 5.35e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKECYsvftNRRPFGPVG---FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQygdV 155
Cdd:cd20621   13 KPLISLVDPEYIKEFLQNHHY----YKKKFGPLGidrLFGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINE---I 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 156 LVRNLRREAETGKPV--TLKHVFGaysmDVITSTSFGVSIDSL-NNPQDPFVENTKKLLRFNPL---DPFVlSIKVFpfl 229
Cdd:cd20621   86 TKEKIKKLDNQNVNIiqFLQKITG----EVVIRSFFGEEAKDLkINGKEIQVELVEILIESFLYrfsSPYF-QLKRL--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 230 tpILEALNITVFPRKV-------ISFLTKSVKQIKEGRLKETQKH--RVDFLQLMIDSQNSKDSETHKALSDLELMAQSI 300
Cdd:cd20621  158 --IFGRKSWKLFPTKKekklqkrVKELRQFIEKIIQNRIKQIKKNkdEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRL-ERVCKK 379
Cdd:cd20621  236 TFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLfPRVATQ 315
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 380 DVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRV 459
Cdd:cd20621  316 DHQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYI 395
                        410       420
                 ....*....|....*....|....
gi 608788355 460 LQNFSFKPCKETQipLKLRFGGLL 483
Cdd:cd20621  396 LKNFEIEIIPNPK--LKLIFKLLY 417
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
80-467 1.23e-67

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: 224.00  E-value: 1.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKECYSVFTNR--RPFGPVgFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEmvpiiaqYGDVLV 157
Cdd:cd11053   24 PVVVLSDPEAIKQIFTADPDVLHPGEgnSLLEPL-LGPNSLLLLDGDRHRRRRKLLMPAFHGERLRA-------YGELIA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 158 RNLRREAET---GKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnPQDPFVENTKKLLRFNPlDPFVLSIKVFPFLTPILE 234
Cdd:cd11053   96 EITEREIDRwppGQPFDLRELMQEITLEVILRVVFGVDDGE---RLQELRRLLPRLLDLLS-SPLASFPALQRDLGPWSP 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 235 ALNITVFPRKVISFLtksVKQIKEGRLKETQKhRVDFLQLMIDSQNSKDSethkALSDLELMAQSIIFIFAGYETTSSVL 314
Cdd:cd11053  172 WGRFLRARRRIDALI---YAEIAERRAEPDAE-RDDILSLLLSARDEDGQ----PLSDEELRDELMTLLFAGHETTATAL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 315 SFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDtvlQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVV 394
Cdd:cd11053  244 AWAFYWLHRHPEVLARLLAELDALGGDPDPEDIA---KLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTTV 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 608788355 395 MIPSYVLHHDPKYWTEPEKFLPERFSKKnkdNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd11053  321 APSIYLTHHRPDLYPDPERFRPERFLGR---KPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLEL 390
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
65-465 3.13e-64

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: 215.28  E-value: 3.13e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  65 YKKYRKVW-GIydcqQPMLAITDPDMIKTVLVKEcySVFTNRRPFGPV--GFMKNAISIAEDEEWKRIRSLLSPTFTSGK 141
Cdd:cd11052   11 YGKNFLYWyGT----DPRLYVTEPELIKELLSKK--EGYFGKSPLQPGlkKLLGRGLVMSNGEKWAKHRRIANPAFHGEK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 LKEMVP-IIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVS-------IDSLNNPQDPFVENTKKLlrF 213
Cdd:cd11052   85 LKGMVPaMVESVSDMLERWKKQMGEEGEEVDVFEEFKALTADIISRTAFGSSyeegkevFKLLRELQKICAQANRDV--G 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 214 NPldpfvlsikvFPFLTPILEALNITVFPRKVISFLTKSVKQiKEGRLKETQK--HRVDFLQLMIDSQNSKDSEthKALS 291
Cdd:cd11052  163 IP----------GSRFLPTKGNKKIKKLDKEIEDSLLEIIKK-REDSLKMGRGddYGDDLLGLLLEANQSDDQN--KNMT 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 292 DLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPtYDTVLQLEYLDMVVNETLRLFPVAM 371
Cdd:cd11052  230 VQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPP-SDSLSKLKTVSMVINESLRLYPPAV 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 372 RLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERFSKK-NKDNIDPYIYTPFGSGPRNCIGMRFAL 449
Cdd:cd11052  309 FLTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGvAKAAKHPMAFLPFGLGPRNCIGQNFAT 388
                        410
                 ....*....|....*.
gi 608788355 450 VNMKLALVRVLQNFSF 465
Cdd:cd11052  389 MEAKIVLAMILQRFSF 404
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
123-489 8.96e-64

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: 214.43  E-value: 8.96e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 123 DEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAEtGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDP 202
Cdd:cd20660   54 GEKWHSRRKMLTPTFHFKILEDFLDVFNEQSEILVKKLKKEVG-KEEFDIFPYITLCALDIICETAMGKSVNAQQNSDSE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 203 FVentKKLLRFNPLdpfVLSIKVFPFLTP---------------ILEALNitVFPRKVI----SFLTKSVKQIKEGRLKE 263
Cdd:cd20660  133 YV---KAVYRMSEL---VQKRQKNPWLWPdfiysltpdgrehkkCLKILH--GFTNKVIqerkAELQKSLEEEEEDDEDA 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 264 T--QKHRVDFLQLMIDSqnskdSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL-P 340
Cdd:cd20660  205 DigKRKRLAFLDLLLEA-----SEEGTKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFgD 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 341 NKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS 420
Cdd:cd20660  280 SDRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFL 359
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 608788355 421 KKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPC-KETQIPLKlrfGGLLLT-EKPI 489
Cdd:cd20660  360 PENSAGRHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSILRNFRIESVqKREDLKPA---GELILRpVDGI 427
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
84-464 9.16e-64

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: 214.50  E-value: 9.16e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVLVKE-----CYSVFTNRRPFGPvgfmkNAISiAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVR 158
Cdd:cd11070   17 VTKPEYLTQIFRRRddfpkPGNQYKIPAFYGP-----NVIS-SEGEDWKRYRKIVAPAFNERNNALVWEESIRQAQRLIR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 159 NLRREA--ETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVEnTKKLLRFNPLDPFVLSikvFPFLtpilEAL 236
Cdd:cd11070   91 YLLEEQpsAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALDEEESSLHD-TLNAIKLAIFPPLFLN---FPFL----DRL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 237 NITVFP------RKVISFLTKSVKQIKEGRLKETQKhrvDFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIFAGYETT 310
Cdd:cd11070  163 PWVLFPsrkrafKDVDEFLSELLDEVEAELSADSKG---KQGTESVVASRLKRARRSGGLTEKELLGNLFIFFIAGHETT 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 311 SSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAP--PTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEI----- 383
Cdd:cd11070  240 ANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDdwDYEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVitglg 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 384 NGMFIPKGVVVMIPSYVLHHDPKYWT-EPEKFLPERFSKKNKDNIDPYI-------YTPFGSGPRNCIGMRFALVNMKLA 455
Cdd:cd11070  320 QEIVIPKGTYVGYNAYATHRDPTIWGpDADEFDPERWGSTSGEIGAATRftpargaFIPFSAGPRACLGRKFALVEFVAA 399

                 ....*....
gi 608788355 456 LVRVLQNFS 464
Cdd:cd11070  400 LAELFRQYE 408
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
82-463 1.48e-63

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: 213.32  E-value: 1.48e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  82 LAITDPDMIKTVLVK-----ECYSVFTNRRPFGPvgfmkNAISIAEDEEWKRIRSLLSPTF--TSGKLKEMVPIIAQYGD 154
Cdd:cd11059   11 VSVNDLDAVREIYGGgfgktKSYWYFTLRGGGGP-----NLFSTLDPKEHSARRRLLSGVYskSSLLRAAMEPIIRERVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKVF-PFLTPIL 233
Cdd:cd11059   86 PLIDRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSRERELLRRLLASLAPWLRWLPRYlPLATSRL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 234 EALNITVFPRKVISFLTKSVKQiKEGRLKETQKHRVDFLQLMIDSQNSKDSethkALSDLELMAQSIIFIFAGYETTSSV 313
Cdd:cd11059  166 IIGIYFRAFDEIEEWALDLCAR-AESSLAESSDSESLTVLLLEKLKGLKKQ----GLDDLEIASEALDHIVAGHDTTAVT 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 314 LSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQ-LEYLDMVVNETLRLF-PVAMRLERVCKKDVE-INGMFIPK 390
Cdd:cd11059  241 LTYLIWELSRPPNLQEKLREELAGLPGPFRGPPDLEDLDkLPYLNAVIRETLRLYpPIPGSLPRVVPEGGAtIGGYYIPG 320
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 608788355 391 GVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPY--IYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd11059  321 GTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETAREMkrAFWPFGSGSRMCIGMNLALMEMKLALAAIYRNY 395
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
79-463 4.47e-63

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: 211.68  E-value: 4.47e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVK-ECYSV-FTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQygdvL 156
Cdd:COG2124   42 GGAWLVTRYEDVREVLRDpRTFSSdGGLPEVLRPLPLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIRE----I 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 157 VRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnpQDPFVENTKKLLR-FNPLDPfvlsikvfPFLTPILEA 235
Cdd:COG2124  118 ADELLDRLAARGPVDLVEEFARPLPVIVICELLGVPEED----RDRLRRWSDALLDaLGPLPP--------ERRRRARRA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 236 LnitvfpRKVISFLTKsvkQIKEGRlketQKHRVDFLQLMIDSQnskdsETHKALSDLELMAQSIIFIFAGYETTSSVLS 315
Cdd:COG2124  186 R------AELDAYLRE---LIAERR----AEPGDDLLSALLAAR-----DDGERLSDEELRDELLLLLLAGHETTANALA 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 316 FIIYELATHPDVQQKVQKEidtvlpnkapptydtvlqLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVM 395
Cdd:COG2124  248 WALYALLRHPEQLARLRAE------------------PELLPAAVEETLRLYPPVPLLPRTATEDVELGGVTIPAGDRVL 309
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 608788355 396 IPSYVLHHDPKYWTEPEKFLPERfskknkdniDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:COG2124  310 LSLAAANRDPRVFPDPDRFDPDR---------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRF 368
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
122-496 1.16e-62

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: 211.27  E-value: 1.16e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 122 EDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAeTGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNP-Q 200
Cdd:cd11068   68 HEPNWGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERLG-PDEPIDVPDDMTRLTLDTIALCGFGYRFNSFYRDeP 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 201 DPFVEntkKLLRFnpLDPFVLSIKVFPFLTPILEALNITVfpRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIdsqN 280
Cdd:cd11068  147 HPFVE---AMVRA--LTEAGRRANRPPILNKLRRRAKRQF--REDIALMRDLVDEIIAERRANPDGSPDDLLNLML---N 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 281 SKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNkAPPTYDTVLQLEYLDMVV 360
Cdd:cd11068  217 GKDPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGD-DPPPYEQVAKLRYIRRVL 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 361 NETLRLFPVAMRLERVCKKDVEINGMF-IPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERFSKKNKDNIDPYIYTPFGSG 438
Cdd:cd11068  296 DETLRLWPTAPAFARKPKEDTVLGGKYpLKKGDPVLVLLPALHRDPSVWGEdAEEFRPERFLPEEFRKLPPNAWKPFGNG 375
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 439 PRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRfggllLTEKP--IVLKAESR 496
Cdd:cd11068  376 QRACIGRQFALQEATLVLAMLLQRFDFEDDPDYELDIKET-----LTLKPdgFRLKARPR 430
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
81-467 3.10e-60

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: 205.29  E-value: 3.10e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  81 MLAITDPDMIKTVLVkecysvfTNRRPFGPVGF--------MKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQY 152
Cdd:cd11046   23 FLVISDPAIAKHVLR-------SNAFSYDKKGLlaeilepiMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRC 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 153 GDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNpQDPFVENTKKLLR--------FNPLDPFVLSIK 224
Cdd:cd11046   96 SERLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTE-ESPVIKAVYLPLVeaehrsvwEPPYWDIPAALF 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 225 VFPFLTPILEALNITvfpRKVISFLTKSVKQI---------KEGRLKETQKHRVDFLQLMIDsqnskDSETHKALSDlEL 295
Cdd:cd11046  175 IVPRQRKFLRDLKLL---NDTLDDLIRKRKEMrqeedielqQEDYLNEDDPSLLRFLVDMRD-----EDVDSKQLRD-DL 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 296 MAqsiiFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLER 375
Cdd:cd11046  246 MT----MLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIR 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 376 VCKKDVEI--NGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDN----IDPYIYTPFGSGPRNCIGMRFAL 449
Cdd:cd11046  322 RAVEDDKLpgGGVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPpnevIDDFAFLPFGGGPRKCLGDQFAL 401
                        410
                 ....*....|....*...
gi 608788355 450 VNMKLALVRVLQNFSFKP 467
Cdd:cd11046  402 LEATVALAMLLRRFDFEL 419
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
77-467 1.85e-59

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: 202.55  E-value: 1.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  77 CQQPMLAITDPDMIKTVLvkecysvftNRRP------------FGPVGFmkNAISIAEDEEWKRIRSLLSPTFTSGKLKE 144
Cdd:cd11083    9 GRQPVLVISDPELIREVL---------RRRPdefrrisslesvFREMGI--NGVFSAEGDAWRRQRRLVMPAFSPKHLRY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 145 MVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLlrFNPLDPFVLSIk 224
Cdd:cd11083   78 FFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQEHLERV--FPMLNRRVNAP- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 225 vFP----FLTPILEALNitvfprKVISFLTKSVKQI-----KEGRLKETQKHRVDFLQLMIDSQNSKDSethkALSDLEL 295
Cdd:cd11083  155 -FPywryLRLPADRALD------RALVEVRALVLDIiaaarARLAANPALAEAPETLLAMMLAEDDPDA----RLTDDEI 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 296 MAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPT-YDTVLQLEYLDMVVNETLRLFPVAMRLE 374
Cdd:cd11083  224 YANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAPLLF 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 375 RVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNK--DNIDPYIYTPFGSGPRNCIGMRFALVNM 452
Cdd:cd11083  304 LEPNEDTVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARaaEPHDPSSLLPFGAGPRLCPGRSLALMEM 383
                        410
                 ....*....|....*
gi 608788355 453 KLALVRVLQNFSFKP 467
Cdd:cd11083  384 KLVFAMLCRNFDIEL 398
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
79-485 2.71e-58

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: 199.41  E-value: 2.71e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKEcySVFTNRRPF----GPvgFMKNAISIAEDEEWKRIRSLLSPTFTSgklkemvPIIAQYGD 154
Cdd:cd11049   23 RPAYVVTSPELVRQVLVND--RVFDKGGPLfdraRP--LLGNGLATCPGEDHRRQRRLMQPAFHR-------SRIPAYAE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNLRREAET---GKPVTLKHVFGAYSMDVITSTSFGVSIDslnnpqDPFVENTKKLLrfnpldPFVLS-IKVFPFLT 230
Cdd:cd11049   92 VMREEAEALAGSwrpGRVVDVDAEMHRLTLRVVARTLFSTDLG------PEAAAELRQAL------PVVLAgMLRRAVPP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 231 PILEALNITVFPR--KVISFLTKSVKQIKEGRlKETQKHRVDFLQLMIDSqnskDSETHKALSDLELMAQSIIFIFAGYE 308
Cdd:cd11049  160 KFLERLPTPGNRRfdRALARLRELVDEIIAEY-RASGTDRDDLLSLLLAA----RDEEGRPLSDEELRDQVITLLTAGTE 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 309 TTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKaPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFI 388
Cdd:cd11049  235 TTASTLAWAFHLLARHPEVERRLHAELDAVLGGR-PATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRL 313
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 389 PKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPC 468
Cdd:cd11049  314 PAGTEVAFSPYALHRDPEVYPDPERFDPDRWLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPV 393
                        410       420
                 ....*....|....*....|.
gi 608788355 469 ----KETQIPLKLRFGGLLLT 485
Cdd:cd11049  394 pgrpVRPRPLATLRPRRLRMR 414
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
79-464 5.70e-58

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: 198.55  E-value: 5.70e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVL---VKEcYSVFTNRRP-FGPvgFMKNAISIAEDEEWKRIRSLLSPTFTsgklKEMVPIIAQYgD 154
Cdd:cd11063   12 TRVIFTIEPENIKAVLatqFKD-FGLGERRRDaFKP--LLGDGIFTSDGEEWKHSRALLRPQFS----RDQISDLELF-E 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNL-RREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVEN------------TKKLLRFNPLDpFVL 221
Cdd:cd11063   84 RHVQNLiKLLPRDGSTVDLQDLFFRLTLDSATEFLFGESVDSLKPGGDSPPAArfaeafdyaqkyLAKRLRLGKLL-WLL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 222 SIKVFPfltpilEALNITvfpRKVISFLTKSVKQIKEGRLKETQKHRVDFL-QLMidsQNSKDsetHKALSDlELMAqsi 300
Cdd:cd11063  163 RDKKFR------EACKVV---HRFVDPYVDKALARKEESKDEESSDRYVFLdELA---KETRD---PKELRD-QLLN--- 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIfAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKD 380
Cdd:cd11063  224 ILL-AGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRD 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 381 VEI------NGM---FIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERFSKKNKdniDPYIYTPFGSGPRNCIGMRFALV 450
Cdd:cd11063  303 TTLprgggpDGKspiFVPKGTRVLYSVYAMHRRKDIWGPdAEEFRPERWEDLKR---PGWEYLPFNGGPRICLGQQFALT 379
                        410
                 ....*....|....
gi 608788355 451 NMKLALVRVLQNFS 464
Cdd:cd11063  380 EASYVLVRLLQTFD 393
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
78-470 9.57e-58

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: 197.48  E-value: 9.57e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  78 QQPMLAITDPDMIKTVLVKecYSVFTN---RRPFGPVGFMKNAISiAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGD 154
Cdd:cd11051    9 APPLLVVTDPELAEQITQV--TNLPKPpplRKFLTPLTGGSSLIS-MEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDS-LNNPQDPFVENTKKLLRFNPLDPFVLSIKVFPFltpil 233
Cdd:cd11051   86 IFAAILRELAESGEVFSLEELTTNLTFDVIGRVTLDIDLHAqTGDNSLLTALRLLLALYRSLLNPFKRLNPLRPL----- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 234 ealnitvfprkvisfltksvKQIKEGRlketqkhRVD-FLQLMIDSQNSKDsethkalsdlELMAQSIIFIFAGYETTSS 312
Cdd:cd11051  161 --------------------RRWRNGR-------RLDrYLKPEVRKRFELE----------RAIDQIKTFLFAGHDTTSS 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 313 VLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPT-------YDTVLQLEYLDMVVNETLRLFPVAMRLeRVCKKDVEI-- 383
Cdd:cd11051  204 TLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAAaellregPELLNQLPYTTAVIKETLRLFPPAGTA-RRGPPGVGLtd 282
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 384 -NGMFIP-KGVVVMIPSYVLHHDPKYWTEPEKFLPERF--SKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRV 459
Cdd:cd11051  283 rDGKEYPtDGCIVYVCHHAIHRDPEYWPRPDEFIPERWlvDEGHELYPPKSAWRPFERGPRNCIGQELAMLELKIILAMT 362
                        410
                 ....*....|.
gi 608788355 460 LQNFSFKPCKE 470
Cdd:cd11051  363 VRRFDFEKAYD 373
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
81-465 1.18e-56

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: 195.11  E-value: 1.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  81 MLAITDPDMIKTV------LVKEcYSVFTNRRPFGPVgfmKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGD 154
Cdd:cd11060   10 EVSISDPEAIKTIygtrspYTKS-DWYKAFRPKDPRK---DNLFSERDEKRHAALRRKVASGYSMSSLLSLEPFVDECID 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 155 VLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQD--PFVENTKKLLrfnpldPFVLSIKVFPFLTPI 232
Cdd:cd11060   86 LLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPFGFLEAGTDvdGYIASIDKLL------PYFAVVGQIPWLDRL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 233 LEaLNITVFPRKVISFLTKSVKQIKE---GRLKETQKH---RVDFLQLMIDSQNSKDSEthkaLSDLELMAQSIIFIFAG 306
Cdd:cd11060  160 LL-KNPLGPKRKDKTGFGPLMRFALEavaERLAEDAESakgRKDMLDSFLEAGLKDPEK----VTDREVVAEALSNILAG 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 307 YETTSSVLSFIIYELATHPDVQQKVQKEIDT-VLPNKA--PPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVC-KKDV 381
Cdd:cd11060  235 SDTTAIALRAILYYLLKNPRVYAKLRAEIDAaVAEGKLssPITFAEAQKLPYLQAVIKEALRLHPpVGLPLERVVpPGGA 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 382 EINGMFIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERF--SKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVR 458
Cdd:cd11060  315 TICGRFIPGGTIVGVNPWVIHRDKEVFGEdADVFRPERWleADEEQRRMMDRADLTFGAGSRTCLGKNIALLELYKVIPE 394

                 ....*..
gi 608788355 459 VLQNFSF 465
Cdd:cd11060  395 LLRRFDF 401
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
79-488 9.89e-56

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: 192.79  E-value: 9.89e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKEcySVFTNRRPFGPVG--FMKNAISIA---EDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYG 153
Cdd:cd11065   12 QTIIVLNSPKAAKDLLEKR--SAIYSSRPRMPMAgeLMGWGMRLLlmpYGPRWRLHRRLFHQLLNPSAVRKYRPLQELES 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 154 DVLVRNLRREAETGKPVtLKHVFGAysmdVITSTSFGVSIDSLNnpqDPFVENTKKLLRFnpldpFVLSIKVFPFLtpil 233
Cdd:cd11065   90 KQLLRDLLESPDDFLDH-IRRYAAS----IILRLAYGYRVPSYD---DPLLRDAEEAMEG-----FSEAGSPGAYL---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 234 ealnITVFP--RKVISFLTKSVKQIKE---GRLKETQKHRVDFLQLMIDSQNSKDS---------ETHKALSDLELMAQS 299
Cdd:cd11065  153 ----VDFFPflRYLPSWLGAPWKRKARelrELTRRLYEGPFEAAKERMASGTATPSfvkdlleelDKEGGLSEEEIKYLA 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 300 IIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCK 378
Cdd:cd11065  229 GSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVApLGIPHALT 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 379 KDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF---SKKNKDNIDPYIYTpFGSGPRNCIGMRFALVNMKLA 455
Cdd:cd11065  309 EDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYlddPKGTPDPPDPPHFA-FGFGRRICPGRHLAENSLFIA 387
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 608788355 456 LVRVLQNFSFKPCKETQ---IPLKLRF-GGLLLTEKP 488
Cdd:cd11065  388 IARLLWAFDIKKPKDEGgkeIPDEPEFtDGLVSHPLP 424
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
66-465 1.74e-54

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: 189.80  E-value: 1.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  66 KKYRKVWGIYDCQQPMLAITDPDMIKTVLVKecYSVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEM 145
Cdd:cd20642    9 KTYGKNSFTWFGPIPRVIIMDPELIKEVLNK--VYDFQKPKTNPLTKLLATGLASYEGDKWAKHRKIINPAFHLEKLKNM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 146 VPIIAQYGDVLVRNLRREAETGKPVTLK--HVFGAYSMDVITSTSFGvsiDSLNNPQDPFvENTKKLLRFNPLDPFVLSI 223
Cdd:cd20642   87 LPAFYLSCSEMISKWEKLVSSKGSCELDvwPELQNLTSDVISRTAFG---SSYEEGKKIF-ELQKEQGELIIQALRKVYI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 224 KVFPFLTPILE------ALNITVFPRKVISfltKSVKQIKEGRLKETqkhrvDFLQLMIDSqNSKDSETHK----ALSDL 293
Cdd:cd20642  163 PGWRFLPTKRNrrmkeiEKEIRSSLRGIIN---KREKAMKAGEATND-----DLLGILLES-NHKEIKEQGnkngGMSTE 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPtYDTVLQLEYLDMVVNETLRLFPVAMRL 373
Cdd:cd20642  234 DVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKPD-FEGLNHLKVVTMILYEVLRLYPPVIQL 312
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 374 ERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEK-FLPERF----SKKNKDNIdpyIYTPFGSGPRNCIGMRFA 448
Cdd:cd20642  313 TRAIHKDTKLGDLTLPAGVQVSLPILLVHRDPELWGDDAKeFNPERFaegiSKATKGQV---SYFPFGWGPRICIGQNFA 389
                        410
                 ....*....|....*..
gi 608788355 449 LVNMKLALVRVLQNFSF 465
Cdd:cd20642  390 LLEAKMALALILQRFSF 406
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
78-467 7.84e-54

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: 187.80  E-value: 7.84e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  78 QQPMLAITDPDMIKTVLVKEcYSVFtnrrPFGPVG------FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKE-MVPIIA 150
Cdd:cd11064   10 GPDGIVTADPANVEHILKTN-FDNY----PKGPEFrdlffdLLGDGIFNVDGELWKFQRKTASHEFSSRALREfMESVVR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 151 QYGDVLVRNLRREA-ETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNN--PQDPFVE-----NTKKLLRFnpldpfvls 222
Cdd:cd11064   85 EKVEKLLVPLLDHAaESGKVVDLQDVLQRFTFDVICKIAFGVDPGSLSPslPEVPFAKafddaSEAVAKRF--------- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 223 iKVFPFLTPILEALNI----------TVFPRKVISFLTKSVKQIKEGrlKETQKHRVDFLQLMIDSqnskdSETHKALSD 292
Cdd:cd11064  156 -IVPPWLWKLKRWLNIgsekklreaiRVIDDFVYEVISRRREELNSR--EEENNVREDLLSRFLAS-----EEEEGEPVS 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 293 LELMAQSII-FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKA-----PPTYDTVLQLEYLDMVVNETLRL 366
Cdd:cd11064  228 DKFLRDIVLnFILAGRDTTAAALTWFFWLLSKNPRVEEKIREELKSKLPKLTtdesrVPTYEELKKLVYLHAALSESLRL 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 367 FPVAMRLERVC-KKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERFSKKNKD--NIDPYIYTPFGSGPRNC 442
Cdd:cd11064  308 YPPVPFDSKEAvNDDVLPDGTFVKKGTRIVYSIYAMGRMESIWGEdALEFKPERWLDEDGGlrPESPYKFPAFNAGPRIC 387
                        410       420
                 ....*....|....*....|....*
gi 608788355 443 IGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd11064  388 LGKDLAYLQMKIVAAAILRRFDFKV 412
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
65-466 8.17e-54

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: 187.49  E-value: 8.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  65 YKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTN-----RRPFGPvgfmkNAISIAEDEEWKRIRSLLSPTFTS 139
Cdd:cd11044   18 YQKYGPVFKTHLLGRPTVFVIGAEAVRFILSGEGKLVRYGwprsvRRLLGE-----NSLSLQDGEEHRRRRKLLAPAFSR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 140 GKLKEMVPIIAQygdvLVRNLRREAETGKPVTLKHVFGAYSMDVITST----SFGVSIDSLNNPQDPFVENtkkllrfnp 215
Cdd:cd11044   93 EALESYVPTIQA----IVQSYLRKWLKAGEVALYPELRRLTFDVAARLllglDPEVEAEALSQDFETWTDG--------- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 216 ldpfVLSIKV-FPFlTPILEALNitvfPR-KVISFLTKSVKQikegRLKETQKHRVDFLQLMIDSQNskdsETHKALSDL 293
Cdd:cd11044  160 ----LFSLPVpLPF-TPFGRAIR----ARnKLLARLEQAIRE----RQEEENAEAKDALGLLLEAKD----EDGEPLSMD 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTvLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRL 373
Cdd:cd11044  223 ELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDA-LGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGG 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 374 ERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSK-KNKDNIDPYIYTPFGSGPRNCIGMRFALVNM 452
Cdd:cd11044  302 FRKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPaRSEDKKKPFSLIPFGGGPRECLGKEFAQLEM 381
                        410
                 ....*....|....
gi 608788355 453 KLALVRVLQNFSFK 466
Cdd:cd11044  382 KILASELLRNYDWE 395
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
78-467 1.99e-53

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: 186.61  E-value: 1.99e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  78 QQPMLAITDPDMIKTVLvKECYSVFTNRrPFGPVG--FMKNAISIA---EDEEWKRIRS-----LLSP----TFTSGKLK 143
Cdd:cd20618   10 SVPTVVVSSPEMAKEVL-KTQDAVFASR-PRTAAGkiFSYNGQDIVfapYGPHWRHLRKictleLFSAkrleSFQGVRKE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 144 EMvpiiaqygDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRfnplDPFVLSI 223
Cdd:cd20618   88 EL--------SHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESEKESEEAREFKELID----EAFELAG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 224 KV-----FPFLTPI----LEALNITVFpRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSethkaLSDLE 294
Cdd:cd20618  156 AFnigdyIPWLRWLdlqgYEKRMKKLH-AKLDRFLQKIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGK-----LSDDN 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 295 LMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTV-----------LPNkapptydtvlqLEYLDMVVNET 363
Cdd:cd20618  230 IKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVvgrerlveesdLPK-----------LPYLQAVVKET 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 364 LRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNI--DPYIYTPFGSGPR 440
Cdd:cd20618  299 LRLHPPGpLLLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVkgQDFELLPFGSGRR 378
                        410       420
                 ....*....|....*....|....*..
gi 608788355 441 NCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd20618  379 MCPGMPLGLRMVQLTLANLLHGFDWSL 405
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
65-466 2.52e-53

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: 186.50  E-value: 2.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  65 YKKYRKVWG----IYDCQQPMLAITDPDMIKTVLVKEcySVFTNRRPFGPVG--FMKNAISIAEDEEWKRIRSLLSPTFT 138
Cdd:cd20639    4 YHHWRKIYGktflYWFGPTPRLTVADPELIREILLTR--ADHFDRYEAHPLVrqLEGDGLVSLRGEKWAHHRRVITPAFH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 139 SGKLKEMVPIIAQYGDVLVRNLRREAETGKP--VTLKHVFGAYSMDVITSTSFGVSIDS---LNNPQDpfventkKLLRF 213
Cdd:cd20639   82 MENLKRLVPHVVKSVADMLDKWEAMAEAGGEgeVDVAEWFQNLTEDVISRTAFGSSYEDgkaVFRLQA-------QQMLL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 214 NPLDPFVLSIKVFPFLtPILEALNITVFPRKVisflTKSVKQIKEGRLKETQKHRV-----DFLQLMIDSQNSKDSEthk 288
Cdd:cd20639  155 AAEAFRKVYIPGYRFL-PTKKNRKSWRLDKEI----RKSLLKLIERRQTAADDEKDdedskDLLGLMISAKNARNGE--- 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 289 ALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP 368
Cdd:cd20639  227 KMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYP 306
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 369 VAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSK-KNKDNIDPYIYTPFGSGPRNCIGMR 446
Cdd:cd20639  307 PAVATIRRAKKDVKLGGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADgVARAAKHPLAFIPFGLGPRTCVGQN 386
                        410       420
                 ....*....|....*....|
gi 608788355 447 FALVNMKLALVRVLQNFSFK 466
Cdd:cd20639  387 LAILEAKLTLAVILQRFEFR 406
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
81-477 6.80e-53

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: 185.56  E-value: 6.80e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  81 MLAITDPDMIKTVLvkecysvftNRR-PFGPVGF------MKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYG 153
Cdd:cd20678   25 FLNIYDPDYAKVVL---------SRSdPKAQGVYkflipwIGKGLLVLNGQKWFQHRRLLTPAFHYDILKPYVKLMADSV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 154 DVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFG----VSIDSLNNPQDPFVENTKKL----LRFNPLDP---FVLS 222
Cdd:cd20678   96 RVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFShqgsCQLDGRSNSYIQAVSDLSNLifqrLRNFFYHNdfiYKLS 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 223 IKVFPFLTPILEALNITVfprKVISFLTKSVKQikEGRLKETQKHR-VDFLQLMIDSQnskdSETHKALSDLELMAQSII 301
Cdd:cd20678  176 PHGRRFRRACQLAHQHTD---KVIQQRKEQLQD--EGELEKIKKKRhLDFLDILLFAK----DENGKSLSDEDLRAEVDT 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 302 FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDV 381
Cdd:cd20678  247 FMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPV 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 382 EI-NGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVL 460
Cdd:cd20678  327 TFpDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTL 406
                        410
                 ....*....|....*..
gi 608788355 461 QNFSFKPcKETQIPLKL 477
Cdd:cd20678  407 LRFELLP-DPTRIPIPI 422
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
80-466 1.55e-52

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: 184.20  E-value: 1.55e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLvKECYSVFTNRRPF-GPVGFMKNAISIA---EDEEWKRIRS-----LLSPTftsgKLKEMVPIIA 150
Cdd:cd11072   14 PTVVVSSPEAAKEVL-KTHDLVFASRPKLlAARILSYGGKDIAfapYGEYWRQMRKicvleLLSAK----RVQSFRSIRE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 151 QYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNnpQDPFVENTKKLLRFnpLDPFVLSiKVFPFLt 230
Cdd:cd11072   89 EEVSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAFGRKYEGKD--QDKFKELVKEALEL--LGGFSVG-DYFPSL- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 231 pilealnitvfprKVISFLTksvkqIKEGRLKETQKhRVD-FLQLMID---SQNSKDSETHKALSDLELMAQ-------- 298
Cdd:cd11072  163 -------------GWIDLLT-----GLDRKLEKVFK-ELDaFLEKIIDehlDKKRSKDEDDDDDDLLDLRLQkegdlefp 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 299 -------SIIF-IF-AGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPV 369
Cdd:cd11072  224 ltrdnikAIILdMFlAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHPP 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 370 A-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKD----NidpYIYTPFGSGPRNCIG 444
Cdd:cd11072  304 ApLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDfkgqD---FELIPFGAGRRICPG 380
                        410       420
                 ....*....|....*....|..
gi 608788355 445 MRFALVNMKLALVRVLQNFSFK 466
Cdd:cd11072  381 ITFGLANVELALANLLYHFDWK 402
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
70-491 6.70e-52

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: 182.42  E-value: 6.70e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  70 KVWGIYDCQQPMLAITDPDMIKTVLVKEcysVFTNRrpfgPVGF--------MKNAISIAEDEEWKRIRSLLSPT---FT 138
Cdd:cd20651    2 DVVGLKLGKDKVVVVSGYEAVREVLSRE---EFDGR----PDGFffrlrtfgKRLGITFTDGPFWKEQRRFVLRHlrdFG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 139 SGKlKEMVPIIAQYGDVLVRNLRREAetGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDP 218
Cdd:cd20651   75 FGR-RSMEEVIQEEAEELIDLLKKGE--KGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKLRKLLELVHLLFRNFDMSG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 219 FVLSIkvFPFLTPIL-EALNITV---FPRKVISFLTKSvkqIKEGRLKETQKHRVDF----LQLMIDSQNSKDSethkaL 290
Cdd:cd20651  152 GLLNQ--FPWLRFIApEFSGYNLlveLNQKLIEFLKEE---IKEHKKTYDEDNPRDLidayLREMKKKEPPSSS-----F 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 291 SDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA 370
Cdd:cd20651  222 TDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLV 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 371 -MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFAL 449
Cdd:cd20651  302 pIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLAR 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 608788355 450 VNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKPIVL 491
Cdd:cd20651  382 NELFLFFTGLLQNFTFSPPNGSLPDLEGIPGGITLSPKPFRV 423
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
79-473 9.23e-51

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: 178.91  E-value: 9.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKEcYSVFTNRRP------FGpvgfmKNAISIAEDEEWKRIRSLLSPTFTSGKLKE-MVPIIaq 151
Cdd:cd11043   16 RPTVVSADPEANRFILQNE-GKLFVSWYPksvrklLG-----KSSLLTVSGEEHKRLRGLLLSFLGPEALKDrLLGDI-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 152 ygDVLVRN-LRREAETGKPVTLKHVfGAYSMDVITSTSFGVS-IDSLNNPQDPFVENTKKLLRFnPLDpfvlsikvFPFl 229
Cdd:cd11043   88 --DELVRQhLDSWWRGKSVVVLELA-KKMTFELICKLLLGIDpEEVVEELRKEFQAFLEGLLSF-PLN--------LPG- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 230 tpilealniTVFPR------KVISFLTKSVKQIKEGRlkETQKHRVDFLQLMIDsqnsKDSETHKALSDLELMAQSIIFI 303
Cdd:cd11043  155 ---------TTFHRalkarkRIRKELKKIIEERRAEL--EKASPKGDLLDVLLE----EKDEDGDSLTDEEILDNILTLL 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 304 FAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP---TYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKD 380
Cdd:cd11043  220 FAGHETTSTTLTLAVKFLAENPKVLQELLEEHEEIAKRKEEGeglTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQD 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 381 VEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFskKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVL 460
Cdd:cd11043  300 VEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW--EGKGKGVPYTFLPFGGGPRLCPGAELAKLEILVFLHHLV 377
                        410
                 ....*....|...
gi 608788355 461 QNFSFKPCKETQI 473
Cdd:cd11043  378 TRFRWEVVPDEKI 390
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
124-463 1.57e-50

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: 179.19  E-value: 1.57e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 124 EEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGK-----PVTLkhvfgaYSMDVITSTSFGVSIDSLNN 198
Cdd:cd20680   66 EKWRSRRKMLTPTFHFTILSDFLEVMNEQSNILVEKLEKHVDGEAfncffDITL------CALDIICETAMGKKIGAQSN 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 199 PQDPFVENTKKLlrfnplDPFVLSIKVFPFLTPIL------------EALNIT-VFPRKVISFLTKSVKQIKEGRL---- 261
Cdd:cd20680  140 KDSEYVQAVYRM------SDIIQRRQKMPWLWLDLwylmfkegkehnKNLKILhTFTDNVIAERAEEMKAEEDKTGdsdg 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 262 -KETQKHRVDFLQLMIdsqNSKDSETHKaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLP 340
Cdd:cd20680  214 eSPSKKKRKAFLDMLL---SVTDEEGNK-LSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFG 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 341 NK-APPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF 419
Cdd:cd20680  290 KSdRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERF 369
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 608788355 420 SKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20680  370 FPENSSGRHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCILRHF 413
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
68-474 4.31e-50

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: 177.79  E-value: 4.31e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNRRPFGPVGFM-KNAISIA-ED--EEWKRIRSLLSPTFT--SGK 141
Cdd:cd11027    1 YGDVFSLYLGSRLVVVLNSGAAIKEALVKK-SADFAGRPKLFTFDLFsRGGKDIAfGDysPTWKLHRKLAHSALRlyASG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 LKEMVPIIAQYGDVLVRNLrrEAETGKPVTLKHVFGAYSMDVITSTSFGVSIDsLNNPQ--------DPFVENTKKllrF 213
Cdd:cd11027   80 GPRLEEKIAEEAEKLLKRL--ASQEGQPFDPKDELFLAVLNVICSITFGKRYK-LDDPEflrlldlnDKFFELLGA---G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 214 NPLDpFVLSIKVFPFLTP-ILEALNITVFprkviSFLTKsvkQIKEGRLKETQKHRVDFLQLMIDSQ---NSKDSETHKA 289
Cdd:cd11027  154 SLLD-IFPFLKYFPNKALrELKELMKERD-----EILRK---KLEEHKETFDPGNIRDLTDALIKAKkeaEDEGDEDSGL 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 290 LSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPV 369
Cdd:cd11027  225 LTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSV 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 370 A-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF-SKKNKDNIDPYIYTPFGSGPRNCIGMRF 447
Cdd:cd11027  305 VpLALPHKTTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFlDENGKLVPKPESFLPFSAGRRVCLGESL 384
                        410       420
                 ....*....|....*....|....*..
gi 608788355 448 ALVNMKLALVRVLQNFSFKPCKETQIP 474
Cdd:cd11027  385 AKAELFLFLARLLQKFRFSPPEGEPPP 411
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
80-467 5.24e-49

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: 175.27  E-value: 5.24e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKECySVFTNRRPFgpVGFMK----NAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDV 155
Cdd:cd20679   24 PIIRLFHPDYIRPVLLASA-AVAPKDELF--YGFLKpwlgDGLLLSSGDKWSRHRRLLTPAFHFNILKPYVKIFNQSTNI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 156 LVRNLRREAETGkPVTL---KHVfGAYSMDVITSTSFgvSIDSlnNPQDPFVENTKKLLRFNPL-----DPFVLSIKVFP 227
Cdd:cd20679  101 MHAKWRRLASEG-SARLdmfEHI-SLMTLDSLQKCVF--SFDS--NCQEKPSEYIAAILELSALvvkrqQQLLLHLDFLY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 228 FLTPilealNITVFPR--KVISFLTKSVkqIKEGRLKETQKHRVDFLQLMIDSQN---------SKDsETHKALSDLELM 296
Cdd:cd20679  175 YLTA-----DGRRFRRacRLVHDFTDAV--IQERRRTLPSQGVDDFLKAKAKSKTldfidvlllSKD-EDGKELSDEDIR 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 297 AQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPT--YDTVLQLEYLDMVVNETLRLFPVAMRLE 374
Cdd:cd20679  247 AEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPEEieWDDLAQLPFLTMCIKESLRLHPPVTAIS 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 375 RVCKKDVEI-NGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMK 453
Cdd:cd20679  327 RCCTQDIVLpDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCIGQTFAMAEMK 406
                        410
                 ....*....|....
gi 608788355 454 LALVRVLQNFSFKP 467
Cdd:cd20679  407 VVLALTLLRFRVLP 420
PLN02290 PLN02290
cytokinin trans-hydroxylase
23-465 1.26e-47

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 173.08  E-value: 1.26e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  23 YLYGTRTHGLFKKLGIPGPTPLPFLGNAL---SFRKGYWTFDMECY----------------KKYRKVWGIYDCQQPMLA 83
Cdd:PLN02290  29 FLTPRRIKKIMERQGVRGPKPRPLTGNILdvsALVSQSTSKDMDSIhhdivgrllphyvawsKQYGKRFIYWNGTEPRLC 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVLVKecYSVFTNR---RPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNL 160
Cdd:PLN02290 109 LTETELIKELLTK--YNTVTGKswlQQQGTKHFIGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSL 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 161 RREAETGKP-VTLKHVFGAYSMDVITSTSFGVSIDS-------LNNPQDPFVENTKKLL----RFNPlDPFVLSIKvfpf 228
Cdd:PLN02290 187 QKAVESGQTeVEIGEYMTRLTADIISRTEFDSSYEKgkqifhlLTVLQRLCAQATRHLCfpgsRFFP-SKYNREIK---- 261
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 229 ltpileALNITVfPRKVISFLTKSVKQIKEGRlkeTQKHRVDFLQLMIDSQNSKDSETHKAlsDLEL-MAQSIIFIFAGY 307
Cdd:PLN02290 262 ------SLKGEV-ERLLMEIIQSRRDCVEIGR---SSSYGDDLLGMLLNEMEKKRSNGFNL--NLQLiMDECKTFFFAGH 329
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 308 ETTSSVLSFIIYELATHPDVQQKVQKEIDTVLpNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMF 387
Cdd:PLN02290 330 ETTALLLTWTLMLLASNPTWQDKVRAEVAEVC-GGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH 408
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 388 IPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSKKNKDNIDPYIytPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:PLN02290 409 IPKGLSIWIPVLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFI--PFAAGPRNCIGQAFAMMEAKIILAMLISKFSF 485
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
97-466 3.25e-47

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: 169.70  E-value: 3.25e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  97 ECYSVFTNrrPFGPVGfmknAISIAEDEEWKRIRSLLSpTFTSGKLKEMVPIIAQYgdvlVRN-LRREAETGkPVTLKHV 175
Cdd:cd11042   42 EVYGFLTP--PFGGGV----VYYAPFAEQKEQLKFGLN-ILRRGKLRGYVPLIVEE----VEKyFAKWGESG-EVDLFEE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 176 FGAYSMDVITSTSFGVSIDSLnnpqdpFVENTKKLLR-----FNPLDPFvlsikvFPFLtpILEALNITVFPRKVIS-FL 249
Cdd:cd11042  110 MSELTILTASRCLLGKEVREL------LDDEFAQLYHdldggFTPIAFF------FPPL--PLPSFRRRDRARAKLKeIF 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 250 TKSVKQikegRLKETQKHRVDFLQLMIDSQnSKDSEthkALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQ 329
Cdd:cd11042  176 SEIIQK----RRKSPDKDEDDMLQTLMDAK-YKDGR---PLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLE 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 330 KVQKEIDTVL-PNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEIN--GMFIPKGVVVMIPSYVLHHDPK 406
Cdd:cd11042  248 ALREEQKEVLgDGDDPLTYDVLKEMPLLHACIKETLRLHPPIHSLMRKARKPFEVEggGYVIPKGHIVLASPAVSHRDPE 327
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 608788355 407 YWTEPEKFLPERFSKKNK--DNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd11042  328 IFKNPDEFDPERFLKGRAedSKGGKFAYLPFGAGRHRCIGENFAYLQIKTILSTLLRNFDFE 389
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
79-470 9.44e-47

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: 168.78  E-value: 9.44e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMIKTVLVKEcySVFTNRRPFGPVGF--MKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVL 156
Cdd:cd20641   22 TPRICISDHELAKQVLSDK--FGFFGKSKARPEILklSGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQVMADCTERM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 157 VRNLRREAETGK----PVTLKHVFGAYSMDVITSTSFGVSidslnnpqdpFVENTKKLLRFNPLDPFVLSIKVFPFLtPI 232
Cdd:cd20641  100 FQEWRKQRNNSEteriEVEVSREFQDLTADIIATTAFGSS----------YAEGIEVFLSQLELQKCAAASLTNLYI-PG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 233 LEAL----NITVfpRKVISFLTKSVKQIKEGRLK-ETQKHRVDFLQLMID--SQNSKDSETHKALSDLELMAQSIIFIFA 305
Cdd:cd20641  169 TQYLptprNLRV--WKLEKKVRNSIKRIIDSRLTsEGKGYGDDLLGLMLEaaSSNEGGRRTERKMSIDEIIDECKTFFFA 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 306 GYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEING 385
Cdd:cd20641  247 GHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKLGG 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 386 MFIPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSKK-NKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20641  327 LEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGvSRAATHPNALLSFSLGPRACIGQNFAMIEAKTVLAMILQRF 406

                 ....*..
gi 608788355 464 SFKPCKE 470
Cdd:cd20641  407 SFSLSPE 413
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
65-472 9.48e-46

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: 166.05  E-value: 9.48e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  65 YKKYRKVWG-IYDCQ---QPMLAITDPDMIKTV-------LVKECYSVFTNRRPFGpvgfmkNAISIAEDEEWKRIRSLL 133
Cdd:cd20640    4 FDKWRKQYGpIFTYStgnKQFLYVSRPEMVKEInlcvsldLGKPSYLKKTLKPLFG------GGILTSNGPHWAHQRKII 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 134 SPTFTSGKLKEMVPIIAQYGDVLVRN----LRREAETGKPVTLKHVFGAYSMDVITSTSFGVSidslnnpqdpFVENTKK 209
Cdd:cd20640   78 APEFFLDKVKGMVDLMVDSAQPLLSSweerIDRAGGMAADIVVDEDLRAFSADVISRACFGSS----------YSKGKEI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 210 LLRFNPLDPFVLSIKVFpFLTPILEAlnitvFPRKV---ISFLTKSVKQ-----IKEGRlkETQKHRVDFLQLMIDSqnS 281
Cdd:cd20640  148 FSKLRELQKAVSKQSVL-FSIPGLRH-----LPTKSnrkIWELEGEIRSlileiVKERE--EECDHEKDLLQAILEG--A 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 282 KDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKaPPTYDTVLQLEYLDMVVN 361
Cdd:cd20640  218 RSSCDKKAEAEDFIVDNCKNIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGG-PPDADSLSRMKTVTMVIQ 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 362 ETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSK-KNKDNIDPYIYTPFGSGP 439
Cdd:cd20640  297 ETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNgVAAACKPPHSYMPFGAGA 376
                        410       420       430
                 ....*....|....*....|....*....|...
gi 608788355 440 RNCIGMRFALVNMKLALVRVLQNFSFKPCKETQ 472
Cdd:cd20640  377 RTCLGQNFAMAELKVLVSLILSKFSFTLSPEYQ 409
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
284-465 1.15e-45

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: 165.18  E-value: 1.15e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 284 SETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVlpNKAPPTYDTVLQLEYLDMVVNET 363
Cdd:cd11045  201 DEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL--GKGTLDYEDLGQLEVTDWVFKEA 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 364 LRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS-KKNKDNIDPYIYTPFGSGPRNC 442
Cdd:cd11045  279 LRLVPPVPTLPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSpERAEDKVHRYAWAPFGGGAHKC 358
                        170       180
                 ....*....|....*....|...
gi 608788355 443 IGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd11045  359 IGLHFAGMEVKAILHQMLRRFRW 381
PTZ00404 PTZ00404
cytochrome P450; Provisional
33-488 4.09e-43

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 159.89  E-value: 4.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  33 FKKLG---IPGPTPLPFLGNALSFRKGYWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNRrPFG 109
Cdd:PTZ00404  23 YKKIHkneLKGPIPIPILGNLHQLGNLPHRDLTKMSKKYGGIFRIWFADLYTVVLSDPILIREMFVDN-FDNFSDR-PKI 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 110 PV---GFMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITS 186
Cdd:PTZ00404 101 PSikhGTFYHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGETFEPRYYLTKFTMSAMFK 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 187 TSFGVSIdslnnPQDPFVENTKKLLRFNPLDpfvlsiKVFPFLT--PILEALNIT-VFPRKVISFLTKSVKQIKEGRLKE 263
Cdd:PTZ00404 181 YIFNEDI-----SFDEDIHNGKLAELMGPME------QVFKDLGsgSLFDVIEITqPLYYQYLEHTDKNFKKIKKFIKEK 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 264 TQKHRV--------DFLQLMIdsqNSKDSETHKALsdLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEI 335
Cdd:PTZ00404 250 YHEHLKtidpevprDLLDLLI---KEYGTNTDDDI--LSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEI 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 336 DTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEI-NGMFIPKGVVVMIPSYVLHHDPKYWTEPEK 413
Cdd:PTZ00404 325 KSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSpFGLPRSTSNDIIIgGGHFIPKDAQILINYYSLGRNEKYFENPEQ 404
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 608788355 414 FLPERFSkkNKDNIDPYIytPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGgllLTEKP 488
Cdd:PTZ00404 405 FDPSRFL--NPDSNDAFM--PFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGKKIDETEEYG---LTLKP 472
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
66-489 1.99e-42

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: 157.00  E-value: 1.99e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  66 KKYRKVWGIYDCQQPMLAITDPDMIKTVLVKE----------CYSVFTNRRpfgpvGFMKNAISiAEDEEWKRIRSLLSP 135
Cdd:cd20647    2 REYGKIFKSHFGPQFVVSIADRDMVAQVLRAEgaapqranmeSWQEYRDLR-----GRSTGLIS-AEGEQWLKMRSVLRQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 136 TFT--------SGKLKEMVPIIAQYgdvlVRNLRREAETGKPVT-LKHVFGAYSMDVITSTSFGVSIDSLNN--PQDPfV 204
Cdd:cd20647   76 KILrprdvavySGGVNEVVADLIKR----IKTLRSQEDDGETVTnVNDLFFKYSMEGVATILYECRLGCLENeiPKQT-V 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 205 ENTKKL-LRFNPLDPFVLSIKVFPFLTPILealnitvfPRKVISFLTKSvkqikEGRLKETQKHrVDFLQLMIDSQNSKD 283
Cdd:cd20647  151 EYIEALeLMFSMFKTTMYAGAIPKWLRPFI--------PKPWEEFCRSW-----DGLFKFSQIH-VDNRLREIQKQMDRG 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 284 SE------TH----KALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQL 353
Cdd:cd20647  217 EEvkggllTYllvsKELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKL 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 354 EYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKK-NKDNIDPYIY 432
Cdd:cd20647  297 PLIRALLKETLRLFPVLPGNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKdALDRVDNFGS 376
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 608788355 433 TPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQiPLKLRFGGLLLTEKPI 489
Cdd:cd20647  377 IPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVSPQTT-EVHAKTHGLLCPGGSI 432
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
80-467 1.64e-41

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: 154.32  E-value: 1.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKEcYSVFTNRRPFGP----VGFMKNAISIAE-DEEWKRIRS-LLSPTFTSGKLKEMVPIIAQYG 153
Cdd:cd11075   14 PLIVVASRELAHEALVQK-GSSFASRPPANPlrvlFSSNKHMVNSSPyGPLWRTLRRnLVSEVLSPSRLKQFRPARRRAL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 154 DVLVRNLRREA-ETGKPVTLKHVFgAYSMDVITST-SFGVSIDslnnpqDPFVENTKKLLR---FNPLDPFVLSIkvFPF 228
Cdd:cd11075   93 DNLVERLREEAkENPGPVNVRDHF-RHALFSLLLYmCFGERLD------EETVRELERVQRellLSFTDFDVRDF--FPA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 229 LTPIL------EALNITVFPRKVISFLTKSVKQIKEGRlketQKHRVDFLQLMIDSQNSKDSETHKALSDLELMAQSIIF 302
Cdd:cd11075  164 LTWLLnrrrwkKVLELRRRQEEVLLPLIRARRKRRASG----EADKDYTDFLLLDLLDLKEEGGERKLTDEELVSLCSEF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 303 IFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLF-PVAMRLERVCKKDV 381
Cdd:cd11075  240 LNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHpPGHFLLPHAVTEDT 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 382 EINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF-SKKNKDNIDP----YIYTPFGSGPRNCIGMRFALVNMKLAL 456
Cdd:cd11075  320 VLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFlAGGEAADIDTgskeIKMMPFGAGRRICPGLGLATLHLELFV 399
                        410
                 ....*....|.
gi 608788355 457 VRVLQNFSFKP 467
Cdd:cd11075  400 ARLVQEFEWKL 410
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
124-492 3.23e-41

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: 153.34  E-value: 3.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 124 EEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETgkPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQ--- 200
Cdd:cd20674   60 LLWKAHRKLTRSALQLGIRNSLEPVVEQLTQELCERMRAQAGT--PVDIQEEFSLLTCSIICCLTFGDKEDKDTLVQafh 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 201 DPFVENTKKLLRfnpldPFVLSIKVFPFL----TPILEALNITVFPRKviSFLTKSVKQIKEGRLKETQKHRVDFLQLMI 276
Cdd:cd20674  138 DCVQELLKTWGH-----WSIQALDSIPFLrffpNPGLRRLKQAVENRD--HIVESQLRQHKESLVAGQWRDMTDYMLQGL 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 277 DSQnsKDSETHKALSDLEL-MAQSIIFIfAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEY 355
Cdd:cd20674  211 GQP--RGEKGMGQLLEGHVhMAVVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPL 287
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 356 LDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVmIPS-YVLHHDPKYWTEPEKFLPERF---SKKNKDNIdpy 430
Cdd:cd20674  288 LNATIAEVLRLRPVVpLALPHRTTRDSSIAGYDIPKGTVV-IPNlQGAHLDETVWEQPHEFRPERFlepGAANRALL--- 363
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 608788355 431 iytPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIP-LKLRFGgllltekpIVLK 492
Cdd:cd20674  364 ---PFGCGARVCLGEPLARLELFVFLARLLQAFTLLPPSDGALPsLQPVAG--------INLK 415
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
66-491 8.77e-41

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: 152.51  E-value: 8.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  66 KKYRKVWGIYDCQQPMLAITDPDMIKTVLVKEC-YSVFTN-----------RRPFGPVgfmknaisIAEDEEWKRIRSLL 133
Cdd:cd20646    2 KIYGPIWKSKFGPYDIVNVASAELIEQVLRQEGkYPMRSDmphwkehrdlrGHAYGPF--------TEEGEKWYRLRSVL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 134 SPTFTsgKLKEMV---PIIAQYGDVLVRNLRREAET-GKPVTLKHVFGA---YSMDVITSTSFGVSIDSLNN--PQDP-- 202
Cdd:cd20646   74 NQRML--KPKEVSlyaDAINEVVSDLMKRIEYLRERsGSGVMVSDLANElykFAFEGISSILFETRIGCLEKeiPEETqk 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 203 FVENTKKLLRFNPLDPFV--LSIKVFPFLTPILEALN-ITVFPRKVISfltKSVKQIkEGRLKETQKHRVDFLQLMIDSQ 279
Cdd:cd20646  152 FIDSIGEMFKLSEIVTLLpkWTRPYLPFWKRYVDAWDtIFSFGKKLID---KKMEEI-EERVDRGEPVEGEYLTYLLSSG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 280 NSKDSETHKALSDLELmaqsiififAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMV 359
Cdd:cd20646  228 KLSPKEVYGSLTELLL---------AGVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAV 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 360 VNETLRLFPVAMRLERVC-KKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSG 438
Cdd:cd20646  299 IKETLRLYPVVPGNARVIvEKEVVVGDYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWLRDGGLKHHPFGSIPFGYG 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 608788355 439 PRNCIGMRFALVNMKLALVRVLQNFSFKPcKETQIPLKLRFGGLLLTEKPIVL 491
Cdd:cd20646  379 VRACVGRRIAELEMYLALSRLIKRFEVRP-DPSGGEVKAITRTLLVPNKPINL 430
PLN02936 PLN02936
epsilon-ring hydroxylase
84-465 2.21e-39

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 149.94  E-value: 2.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVL-----------VKECySVFTnrrpFGpVGFmknaiSIAEDEEWKRIRSLLSPTFTSGKLKEMVP-IIAQ 151
Cdd:PLN02936  65 VSDPAIAKHVLrnygskyakglVAEV-SEFL----FG-SGF-----AIAEGELWTARRRAVVPSLHRRYLSVMVDrVFCK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 152 YGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNpQDPFVENTKKLL-----RFNPLDPFvlsIKVf 226
Cdd:PLN02936 134 CAERLVEKLEPVALSGEAVNMEAKFSQLTLDVIGLSVFNYNFDSLTT-DSPVIQAVYTALkeaetRSTDLLPY---WKV- 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 227 PFLTPILealnitvfPRKVISflTKSVKQIKE--GRLKETQKHRVDFLQLMIDSQ---NSKDSETHKAL-------SDLE 294
Cdd:PLN02936 209 DFLCKIS--------PRQIKA--EKAVTVIREtvEDLVDKCKEIVEAEGEVIEGEeyvNDSDPSVLRFLlasreevSSVQ 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 295 LMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKaPPTYDTVLQLEYLDMVVNETLRLFP---VAM 371
Cdd:PLN02936 279 LRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGR-PPTYEDIKELKYLTRCINESMRLYPhppVLI 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 372 RLERVckKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS----KKNKDNIDpYIYTPFGSGPRNCIGMRF 447
Cdd:PLN02936 358 RRAQV--EDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERFDldgpVPNETNTD-FRYIPFSGGPRKCVGDQF 434
                        410
                 ....*....|....*...
gi 608788355 448 ALVNMKLALVRVLQNFSF 465
Cdd:PLN02936 435 ALLEAIVALAVLLQRLDL 452
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
225-487 7.08e-39

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: 147.08  E-value: 7.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 225 VFPFLTpilealnitVFPRKVISFLTKSVKQIKEGRLKETQKHRVDF--------LQLMI------DSQNSKDSETHKAL 290
Cdd:cd20673  158 IFPWLQ---------IFPNKDLEKLKQCVKIRDKLLQKKLEEHKEKFssdsirdlLDALLqakmnaENNNAGPDQDSVGL 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 291 SDLELMAqSIIFIF-AGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPV 369
Cdd:cd20673  229 SDDHILM-TVGDIFgAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPV 307
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 370 A-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF-SKKNKDNIDPYI-YTPFGSGPRNCIGMR 446
Cdd:cd20673  308 ApLLIPHVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFlDPTGSQLISPSLsYLPFGAGPRVCLGEA 387
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 608788355 447 FALVNMKLALVRVLQNFSFKPCKETQIP-LKLRFGGLLLTEK 487
Cdd:cd20673  388 LARQELFLFMAWLLQRFDLEVPDGGQLPsLEGKFGVVLQIDP 429
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
121-491 1.08e-38

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: 146.82  E-value: 1.08e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 121 AEDEEWKRIRSLLSPTFTsgKLKEmvpiIAQYGDV-------LVRNLRREAETGKPVTLKHV---FGAYSMDVITSTSFG 190
Cdd:cd20648   62 AEGEEWQRLRSLLAKHML--KPKA----VEAYAGVlnavvtdLIRRLRRQRSRSSPGVVKDIageFYKFGLEGISSVLFE 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 191 VSIDSLNnPQDPfvENTKKLLR-FNPLDPFVLSIKVFP-FLTPILEAL---------NITVFPRKVISFLTKSVKQIKEG 259
Cdd:cd20648  136 SRIGCLE-ANVP--EETETFIQsINTMFVMTLLTMAMPkWLHRLFPKPwqrfcrswdQMFAFAKGHIDRRMAEVAAKLPR 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 260 RLKETQKHRVDFLqlmidsqnskdsethkalSDLELMAQSII-----FIFAGYETTSSVLSFIIYELATHPDVQQKVQKE 334
Cdd:cd20648  213 GEAIEGKYLTYFL------------------AREKLPMKSIYgnvteLLLAGVDTISSTLSWSLYELSRHPDVQTALHRE 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 335 IDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVC-KKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEK 413
Cdd:cd20648  275 ITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIpDRDIQVGEYIIPKKTLITLCHYATSRDENQFPDPNS 354
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 608788355 414 FLPERFSKKNkDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQiPLKLRFGGLLLTEKPIVL 491
Cdd:cd20648  355 FRPERWLGKG-DTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVRPEPGGS-PVKPMTRTLLVPERSINL 430
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
84-466 1.58e-38

cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant cytochrome P450 family 76 (CYP76 or Cyp76) include: Catharanthus roseus CYP76B6, a multifunctional enzyme catalyzing two sequential oxidation steps leading to the formation of 8-oxogeraniol from geraniol; the Brassicaceae-specific CYP76C subfamily of enzymes that are involved in the metabolism of monoterpenols and phenylurea herbicides; and two P450s from Lamiaceae, CYP76AH and CYP76AK, that are involved in the oxidation of abietane diterpenes. CYP76AH produces ferruginol and 11-hydroxyferruginol, while CYP76AK catalyzes oxidations at the C20 position. Also included in this group is Berberis stolonifera Cyp80, also called berbamunine synthase or (S)-N-methylcoclaurine oxidase [C-O phenol-coupling], that catalyzes the phenol oxidation of N-methylcoclaurine to form the bisbenzylisoquinoline alkaloid berbamunine. The CYP76-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 146.14  E-value: 1.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVLVKEcYSVFTNRRPFGPV---GFMKNAISIAE-DEEWKRIRSLL-SPTFTSGKLKEMVPIIAQYGDVLVR 158
Cdd:cd11073   20 VSSPEAAREVLKTH-DRVLSGRDVPDAVralGHHKSSIVWPPyGPRWRMLRKICtTELFSPKRLDATQPLRRRKVRELVR 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 159 NLRREAETGKPVTLKH-VFGAySMDVITSTSFGVSIDSLNNP-----QDPFVENTKKLLRFNPLDpfvlsikVFPFLTPI 232
Cdd:cd11073   99 YVREKAGSGEAVDIGRaAFLT-SLNLISNTLFSVDLVDPDSEsgsefKELVREIMELAGKPNVAD-------FFPFLKFL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 233 -LEAL--NITVFPRKVISFLTKSVKQ-IKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKALSDLeLMAqsiIFIfAGYE 308
Cdd:cd11073  171 dLQGLrrRMAEHFGKLFDIFDGFIDErLAEREAGGDKKKDDDLLLLLDLELDSESELTRNHIKAL-LLD---LFV-AGTD 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 309 TTSSVLSFIIYELATHPDVQQKVQKEIDTVL-PNKAPPTYDtVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGM 386
Cdd:cd11073  246 TTSSTIEWAMAELLRNPEKMAKARAELDEVIgKDKIVEESD-ISKLPYLQAVVKETLRLHPPApLLLPRKAEEDVEVMGY 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 387 FIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKN-----KDnidpYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQ 461
Cdd:cd11073  325 TIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEidfkgRD----FELIPFGSGRRICPGLPLAERMVHLVLASLLH 400

                 ....*
gi 608788355 462 NFSFK 466
Cdd:cd11073  401 SFDWK 405
PLN02738 PLN02738
carotene beta-ring hydroxylase
121-466 5.49e-38

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 147.75  E-value: 5.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 121 AEDEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNpQ 200
Cdd:PLN02738 217 ADGEIWRVRRRAIVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDSLSN-D 295
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 201 DPFVENTKKLLRfnplDPFVLSIKVFPFL-TPILEAlnITVFPRKVisflTKSVKQIKE--GRLKETQKHRVDF--LQLM 275
Cdd:PLN02738 296 TGIVEAVYTVLR----EAEDRSVSPIPVWeIPIWKD--ISPRQRKV----AEALKLINDtlDDLIAICKRMVEEeeLQFH 365
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 276 IDSQNSKD-SETH-----------KALSDlELMAQSIififAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKA 343
Cdd:PLN02738 366 EEYMNERDpSILHfllasgddvssKQLRD-DLMTMLI----AGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRF 440
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 344 pPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF---- 419
Cdd:PLN02738 441 -PTIEDMKKLKYTTRVINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpldg 519
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 608788355 420 SKKNKDNIDpYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:PLN02738 520 PNPNETNQN-FSYLPFGGGPRKCVGDMFASFENVVATAMLVRRFDFQ 565
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
70-488 3.00e-37

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: 142.55  E-value: 3.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  70 KVWGIYDCQQPMLAITDPDMIKTVLVKEcysVFTNRRP-FGPVGFMK-NAISIAEDEEWKRIRSLLSP-------TFTSG 140
Cdd:cd20652    2 SIFSLKMGSVYTVVLSDPKLIRDTFRRD---EFTGRAPlYLTHGIMGgNGIICAEGDLWRDQRRFVHDwlrqfgmTKFGN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 141 KLKEMVPIIAQYGDVLVRNLrrEAETGKPVTLKHVFGAYSMDVITSTSFGVSidslnnpqdpFVENTKKLLRFNPLDP-- 218
Cdd:cd20652   79 GRAKMEKRIATGVHELIKHL--KAESGQPVDPSPVLMHSLGNVINDLVFGFR----------YKEDDPTWRWLRFLQEeg 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 219 --FVLSIKVFPFLtPILEALNITvfpRKVISFLTKSVKQIKEGRLKETQKHRVDFL----QLMIDSQNSKDSETHKALSD 292
Cdd:cd20652  147 tkLIGVAGPVNFL-PFLRHLPSY---KKAIEFLVQGQAKTHAIYQKIIDEHKRRLKpenpRDAEDFELCELEKAKKEGED 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 293 LELMAQS---------IIFIF-AGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNE 362
Cdd:cd20652  223 RDLFDGFytdeqlhhlLADLFgAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISE 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 363 TLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRN 441
Cdd:cd20652  303 SQRIRSVVpLGIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRM 382
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 608788355 442 CIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKP 488
Cdd:cd20652  383 CLGDELARMILFLFTARILRKFRIALPDGQPVDSEGGNVGITLTPPP 429
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
80-493 4.70e-37

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: 142.05  E-value: 4.70e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKECySVFTNRRPFGPVGFMKNAISIA---EDEEWKRIRSLLSP---TFTSGK----LKEMVPII 149
Cdd:cd11028   13 PVVVLNGLETIKQALVRQG-EDFAGRPDFYSFQFISNGKSMAfsdYGPRWKLHRKLAQNalrTFSNARthnpLEEHVTEE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 150 AQYgdvLVRNL-RREAETGKPVTLKHVFGAYSmDVITSTSFGVSIDsLNNP--QDpFVENTKKLLRF----NPLDpfvls 222
Cdd:cd11028   92 AEE---LVTELtENNGKPGPFDPRNEIYLSVG-NVICAICFGKRYS-RDDPefLE-LVKSNDDFGAFvgagNPVD----- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 223 ikVFPFLTPilealnitVFPRKVISF--LTKSV-----KQIKEGRLKETQKHRVDFLQLMIDSQNSKDSETHKA--LSDL 293
Cdd:cd11028  161 --VMPWLRY--------LTRRKLQKFkeLLNRLnsfilKKVKEHLDTYDKGHIRDITDALIKASEEKPEEEKPEvgLTDE 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLR---LFPVA 370
Cdd:cd11028  231 HIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRhssFVPFT 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 371 mrLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF----SKKNKDNIDPYIytPFGSGPRNCIGMR 446
Cdd:cd11028  311 --IPHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFlddnGLLDKTKVDKFL--PFGAGRRRCLGEE 386
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 608788355 447 FALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGgllLTEKPIVLKA 493
Cdd:cd11028  387 LARMELFLFFATLLQQCEFSVKPGEKLDLTPIYG---LTMKPKPFKV 430
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
68-488 6.72e-37

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: 141.54  E-value: 6.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKECySVFTNRRPFgPVgFMK----NAISIAEDEEWKRIR--SLLS-PTFTSG 140
Cdd:cd11026    1 YGPVFTVYLGSKPVVVLCGYEAVKEALVDQA-EEFSGRPPV-PL-FDRvtkgYGVVFSNGERWKQLRrfSLTTlRNFGMG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 141 KlKEMVPIIAQYGDVLVRNLRREaeTGKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnpQDPFVentKKLLR-FNPLDPF 219
Cdd:cd11026   78 K-RSIEERIQEEAKFLVEAFRKT--KGKPFDPTFLLSNAVSNVICSIVFGSRFDY----EDKEF---LKLLDlINENLRL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 220 VLS--IKVFPFLTPILEAL-----NITVFPRKVISFLTKSVKQIKEGRLKETQKHRVD-FLQLMidSQNSKDSETHkaLS 291
Cdd:cd11026  148 LSSpwGQLYNMFPPLLKHLpgphqKLFRNVEEIKSFIRELVEEHRETLDPSSPRDFIDcFLLKM--EKEKDNPNSE--FH 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 292 DLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VA 370
Cdd:cd11026  224 EENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDiVP 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 371 MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALV 450
Cdd:cd11026  304 LGVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARM 383
                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 608788355 451 NMKLALVRVLQNFSFK-PCKETQIPLKLRFGGLLLTEKP 488
Cdd:cd11026  384 ELFLFFTSLLQRFSLSsPVGPKDPDLTPRFSGFTNSPRP 422
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
223-484 7.63e-37

cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This family is composed of predominantly fungal cytochrome P450s (CYPs) with similarity to Fusarium fujikuroi Cytochrome P450 503A1 (CYP503A1, also called ent-kaurene oxidase or cytochrome P450-4), Aspergillus nidulans austinol synthesis protein I (ausI), Alternaria alternata tentoxin synthesis protein 1 (TES1), and Acanthamoeba polyphaga mimivirus cytochrome P450 51 (CYP51, also called P450-LIA1 or sterol 14-alpha demethylase). Ent-kaurene oxidase catalyzes three successive oxidations of the 4-methyl group of ent-kaurene to form kaurenoic acid, an intermediate in gibberellin biosynthesis. AusI and TES1 are cytochrome P450 monooxygenases that mediate the biosynthesis of the meroterpenoids, austinol and dehydroaustinol, and the phytotoxin tentoxin, respectively. P450-LIA1 catalyzes the 14-alpha demethylation of obtusifoliol and functions in steroid biosynthesis. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 141.66  E-value: 7.63e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 223 IKVFP-FLTPILEalNITVFPRKVISFLTKSV--------KQIKEGRLKETQKHrVDFLQLMIDSQNSKDSEThkalsdL 293
Cdd:cd11041  155 LRLFPpFLRPLVA--PFLPEPRRLRRLLRRARpliipeieRRRKLKKGPKEDKP-NDLLQWLIEAAKGEGERT------P 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAQSIIFI-FAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMR 372
Cdd:cd11041  226 YDLADRQLALsFAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLV 305
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 373 -LERVCKKDVEI-NGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYT---------PFGSGPRN 441
Cdd:cd11041  306 sLRRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRLREQPGQEKKHQfvstspdflGFGHGRHA 385
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 608788355 442 CIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLL 484
Cdd:cd11041  386 CPGRFFASNEIKLILAHLLLNYDFKLPEGGERPKNIWFGEFIM 428
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
116-470 1.19e-35

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: 139.36  E-value: 1.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 116 NAISIAEDEEWKRIRSLLSPTFTSGKLKEMV-PIIAQYGDVLVRNLRREAE--TGKPVTLKHVFGAYSMDVITSTSFGVS 192
Cdd:cd20622   52 HHLVKSTGPAFRKHRSLVQDLMTPSFLHNVAaPAIHSKFLDLIDLWEAKARlaKGRPFSAKEDIHHAALDAIWAFAFGIN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 193 ID-SLNNPQDPFVENTKKL---------LRFnPLDPFVLSIKVFPFLTPILEALNITVFPRKVISFLTKSVKQIKEGRLK 262
Cdd:cd20622  132 FDaSQTRPQLELLEAEDSTilpagldepVEF-PEAPLPDELEAVLDLADSVEKSIKSPFPKLSHWFYRNQPSYRRAAKIK 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 263 EtqkhrvDFLQLMIDSQN---SKDSETHKALSDLELMAQ-----------------SII------FIFAGYETTSSVLSF 316
Cdd:cd20622  211 D------DFLQREIQAIArslERKGDEGEVRSAVDHMVRrelaaaekegrkpdyysQVIhdelfgYLIAGHDTTSTALSW 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 317 IIYELATHPDVQQKVQKEIDTVLP----NKAPPTYDTVLQ--LEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPK 390
Cdd:cd20622  285 GLKYLTANQDVQSKLRKALYSAHPeavaEGRLPTAQEIAQarIPYLDAVIEEILRCANTAPILSREATVDTQVLGYSIPK 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 391 GVVVM----IPSYV---LHHD------------PKYWT----EPEKFLPERFSKKNKD------NIDPYIYTPFGSGPRN 441
Cdd:cd20622  365 GTNVFllnnGPSYLsppIEIDesrrssssaakgKKAGVwdskDIADFDPERWLVTDEEtgetvfDPSAGPTLAFGLGPRG 444
                        410       420
                 ....*....|....*....|....*....
gi 608788355 442 CIGMRFALVNMKLALVRVLQNFSFKPCKE 470
Cdd:cd20622  445 CFGRRLAYLEMRLIITLLVWNFELLPLPE 473
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
107-491 4.00e-35

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: 136.57  E-value: 4.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 107 PFGP-VGFMKNaISIAEdeewkrirsLLSPTftsgKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVIT 185
Cdd:cd20655   56 PYGDyWKFMKK-LCMTE---------LLGPR----ALERFRPIRAQELERFLRRLLDKAEKGESVDIGKELMKLTNNIIC 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 186 STSFGVSIDSLNNPqdpfVENTKKLLRfnplDPFVLSIKVF--PFLTPiLEALNITVFPRKVIS-------FLTKSVKQI 256
Cdd:cd20655  122 RMIMGRSCSEENGE----AEEVRKLVK----ESAELAGKFNasDFIWP-LKKLDLQGFGKRIMDvsnrfdeLLERIIKEH 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 257 KEGRLKETQKHRVDFLQLMIDSQNSKDSE-----TH-KALsdlelmaqsIIFIF-AGYETTSSVLSFIIYELATHPDVQQ 329
Cdd:cd20655  193 EEKRKKRKEGGSKDLLDILLDAYEDENAEykitrNHiKAF---------ILDLFiAGTDTSAATTEWAMAELINNPEVLE 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 330 KVQKEIDTV-----------LPNkapptydtvlqLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPS 398
Cdd:cd20655  264 KAREEIDSVvgktrlvqesdLPN-----------LPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLFVNV 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 399 YVLHHDPKYWTEPEKFLPERF--SKKNKDNIDP----YIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQ 472
Cdd:cd20655  333 YAIMRDPNYWEDPLEFKPERFlaSSRSGQELDVrgqhFKLLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDWKVGDGEK 412
                        410
                 ....*....|....*....
gi 608788355 473 IPLKLRFGGLLLTEKPIVL 491
Cdd:cd20655  413 VNMEEASGLTLPRAHPLKC 431
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
80-467 5.68e-34

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: 133.22  E-value: 5.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKecySVFTNRrpfgPV-----GFMKN-AISIAE-DEEWKRIRS-----LLSP--TFTSGKLKEM 145
Cdd:cd11076   14 RVVITSHPETAREILNS---PAFADR----PVkesayELMFNrAIGFAPyGEYWRNLRRiasnhLFSPrrIAASEPQRQA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 146 VpiiaqyGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDpfVENTKKLLR--FNPLDPFVLSi 223
Cdd:cd11076   87 I------AAQMVKAIAKEMERSGEVAVRKHLQRASLNNIMGSVFGRRYDFEAGNEE--AEELGEMVRegYELLGAFNWS- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 224 KVFPFLTPiLEALNITVFPRKVISFLTKSVKQ-IKEGRLKETQKHRVDFL--QLMIDSQNskdsetHKALSDLELMAQSI 300
Cdd:cd11076  158 DHLPWLRW-LDLQGIRRRCSALVPRVNTFVGKiIEEHRAKRSNRARDDEDdvDVLLSLQG------EEKLSDSDMIAVLW 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLE--RVCK 378
Cdd:cd11076  231 EMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAKLPYLQAVVKETLRLHPPGPLLSwaRLAI 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 379 KDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDN------IDPYIyTPFGSGPRNCIGMRFALVNM 452
Cdd:cd11076  311 HDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGAdvsvlgSDLRL-APFGAGRRVCPGKALGLATV 389
                        410
                 ....*....|....*
gi 608788355 453 KLALVRVLQNFSFKP 467
Cdd:cd11076  390 HLWVAQLLHEFEWLP 404
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
68-488 6.21e-34

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: 133.36  E-value: 6.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKECySVFTNR-----------------RPFGPVgfmknaisiaedeeWKRIR 130
Cdd:cd20666    1 YGNIFSLFIGSQLVVVLNDFESVREALVQKA-EVFSDRpsvplvtiltkgkgivfAPYGPV--------------WRQQR 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 131 SLLSPT---FTSGKLKEMVPIIAQYGDVLVRNLRREaetGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDPFVENT 207
Cdd:cd20666   66 KFSHSTlrhFGLGKLSLEPKIIEEFRYVKAEMLKHG---GDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFKTMLGLM 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 208 KKLLRFNpLDPFVLSIKVFPFL--TPILEALNITVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSE 285
Cdd:cd20666  143 SRGLEIS-VNSAAILVNICPWLyyLPFGPFRELRQIEKDITAFLKKIIADHRETLDPANPRDFIDMYLLHIEEEQKNNAE 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 286 ThkALSDLELMaqSII--FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL-PNKAPPTYDTVlQLEYLDMVVNE 362
Cdd:cd20666  222 S--SFNEDYLF--YIIgdLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIgPDRAPSLTDKA-QMPFTEATIME 296
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 363 TLRLFPV-AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRN 441
Cdd:cd20666  297 VQRMTVVvPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRV 376
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 608788355 442 CIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFGGLLLTEKP 488
Cdd:cd20666  377 CMGEQLAKMELFLMFVSLMQSFTFLLPPNAPKPSMEGRFGLTLAPCP 423
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
79-466 6.82e-34

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: 133.51  E-value: 6.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  79 QPMLAITDPDMiktvlVKECYSV----FTNRRP---------------FGPVGfmknaisiaedEEWKRIR-----SLLS 134
Cdd:cd20654   11 HPTLVVSSWEM-----AKECFTTndkaFSSRPKtaaaklmgynyamfgFAPYG-----------PYWRELRkiatlELLS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 135 PTftsgKLKEMVPIIAQYGDVLVRNL------RREAETGKPVTLKHVFGAYSMDVITST-----SFGVSIDSLNNPQDPF 203
Cdd:cd20654   75 NR----RLEKLKHVRVSEVDTSIKELyslwsnNKKGGGGVLVEMKQWFADLTFNVILRMvvgkrYFGGTAVEDDEEAERY 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 204 VENTKKLLRFnpLDPFVLSIkVFPFLTPI-----LEALNITVfpRKVISFLTKSVKQIKEGRL--KETQKHRVDFLQLMI 276
Cdd:cd20654  151 KKAIREFMRL--AGTFVVSD-AIPFLGWLdfgghEKAMKRTA--KELDSILEEWLEEHRQKRSssGKSKNDEDDDDVMML 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 277 DSQNSKDSETHKAlsDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYL 356
Cdd:cd20654  226 SILEDSQISGYDA--DTVIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 357 DMVVNETLRLFPVAMRL-ERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF--SKKNKDNIDP-YIY 432
Cdd:cd20654  304 QAIVKETLRLYPPGPLLgPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFltTHKDIDVRGQnFEL 383
                        410       420       430
                 ....*....|....*....|....*....|....
gi 608788355 433 TPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20654  384 IPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIK 417
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
244-480 4.69e-33

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: 131.09  E-value: 4.69e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 244 KVISFLTKSVKQIKEGRLKETQKHRVD-FLQLMidSQNSKDSETHKALSDLELMAQSIIFifAGYETTSSVLSFIIYELA 322
Cdd:cd20661  191 EVYDFLLRLIERFSENRKPQSPRHFIDaYLDEM--DQNKNDPESTFSMENLIFSVGELII--AGTETTTNVLRWAILFMA 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 323 THPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVL 401
Cdd:cd20661  267 LYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVpLGIFHATSKDAVVRGYSIPKGTTVITNLYSV 346
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 402 HHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG 480
Cdd:cd20661  347 HFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGLIPDLKPKLG 425
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
65-463 1.13e-32

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: 129.54  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  65 YKKYRKVW----GIYDCQQpmlaITDPDMIKTVLVKEcySVFTNRRPFGPVGFMKN------AISIAEDEEWKRIRS--- 131
Cdd:cd20645    1 HKKFGKIFrmklGSFESVH----IGSPCLLEALYRKE--SAYPQRLEIKPWKAYRDyrdeayGLLILEGQEWQRVRSafq 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 132 --LLSPTFT---SGKLKEMVPIIAQYGDVLVrnlrreAETGKPVTLKHVFGAYSMD----VITSTSFGVSIDSLNNPQDP 202
Cdd:cd20645   75 kkLMKPKEVmklDGKINEVLADFMGRIDELC------DETGRVEDLYSELNKWSFEticlVLYDKRFGLLQQNVEEEALN 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 203 FVENTKKLLR-FNPLdpfvlsikvfpFLTPIL--EALNITVFPRKVISF--LTKSVKQIKEGRL-KETQKHRVDFLQLMI 276
Cdd:cd20645  149 FIKAIKTMMStFGKM-----------MVTPVElhKRLNTKVWQDHTEAWdnIFKTAKHCIDKRLqRYSQGPANDFLCDIY 217
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 277 DSQNSKDSETHKALSDLELmaqsiififAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYL 356
Cdd:cd20645  218 HDNELSKKELYAAITELQI---------GGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLPANQTPRAEDLKNMPYL 288
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 357 DMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKnKDNIDPYIYTPFG 436
Cdd:cd20645  289 KACLKESMRLTPSVPFTSRTLDKDTVLGDYLLPKGTVLMINSQALGSSEEYFEDGRQFKPERWLQE-KHSINPFAHVPFG 367
                        410       420
                 ....*....|....*....|....*..
gi 608788355 437 SGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20645  368 IGKRMCIGRRLAELQLQLALCWIIQKY 394
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
81-466 8.96e-32

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: 126.98  E-value: 8.96e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  81 MLAITDPDMiktvlvkeCYSVFTNRRP--FGPVG-------FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPI--- 148
Cdd:cd11082   12 IVFVTDAEL--------SRKIFSNNRPdaFHLCLhpnakkiLGEDNLIFMFGEEHKELRKSLLPLFTRKALGLYLPIqer 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 149 -IAQYgdvLVRNLRREAETGKPVTLKHVFgaysMDVITSTSFGVSI-DSLNNPQDPFVEN----TKKLLRFnPLDpfvls 222
Cdd:cd11082   84 vIRKH---LAKWLENSKSGDKPIEMRPLI----RDLNLETSQTVFVgPYLDDEARRFRIDynyfNVGFLAL-PVD----- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 223 ikvFPFLtpileALNITVFPRKVI-SFLTKSVKQIKEgRLKETQKHR--VDF-LQLMIDSQNSKD---SETHKALSDLEl 295
Cdd:cd11082  151 ---FPGT-----ALWKAIQARKRIvKTLEKCAAKSKK-RMAAGEEPTclLDFwTHEILEEIKEAEeegEPPPPHSSDEE- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 296 MAQSII-FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP-TYDTVLQLEYLDMVVNETLRLFPVAMRL 373
Cdd:cd11082  221 IAGTLLdFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEPPlTLDLLEEMKYTRQVVKEVLRYRPPAPMV 300
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 374 ERVCKKDVEINGMF-IPKGVVVmIPS-YVLHHDPkyWTEPEKFLPERFSKKNK-DNIDPYIYTPFGSGPRNCIGMRFALV 450
Cdd:cd11082  301 PHIAKKDFPLTEDYtVPKGTIV-IPSiYDSCFQG--FPEPDKFDPDRFSPERQeDRKYKKNFLVFGAGPHQCVGQEYAIN 377
                        410
                 ....*....|....*.
gi 608788355 451 NMKLALVRVLQNFSFK 466
Cdd:cd11082  378 HLMLFLALFSTLVDWK 393
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
258-466 1.10e-31

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: 126.57  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 258 EGRLKETQKHRVDFLQLMIDSQ-NSKDSETHKALSDLELMAQS--------II------FIFAGYETTSSVLSFIIYELA 322
Cdd:cd20653  176 EKRVKKLAKRRDAFLQGLIDEHrKNKESGKNTMIDHLLSLQESqpeyytdeIIkglilvMLLAGTDTSAVTLEWAMSNLL 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 323 THPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVL 401
Cdd:cd20653  256 NHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAApLLVPHESSEDCKIGGYDIPRGTMLLVNAWAI 335
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 608788355 402 HHDPKYWTEPEKFLPERFSKKNKDNidpYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20653  336 HRDPKLWEDPTKFKPERFEGEEREG---YKLIPFGLGRRACPGAGLAQRVVGLALGSLIQCFEWE 397
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
68-480 7.47e-31

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: 124.52  E-value: 7.47e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSvFTNRRPFgPVG---FMKNAISIAEDEEWKRIRSLLSPT---FTSGK 141
Cdd:cd20662    1 YGNIFSLQLGSISSVIVTGLPLIKEALVTQEQN-FMNRPET-PLReriFNKNGLIFSSGQTWKEQRRFALMTlrnFGLGK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 lKEMVPIIAQYGDVLVRNLRreAETGKPVT--LKhVFGAYSmDVITSTSFGVSIDSlnnpQDpfvENTKKLLRFnpLD-- 217
Cdd:cd20662   79 -KSLEERIQEECRHLVEAIR--EEKGNPFNphFK-INNAVS-NIICSVTFGERFEY----HD---EWFQELLRL--LDet 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 218 ------PFVLSIKVFPFLTPILEALNITVFP--RKVISFLTKSVKQIKEGRLKETQKHRVD-FLQLMidsqnSKDSETHK 288
Cdd:cd20662  145 vylegsPMSQLYNAFPWIMKYLPGSHQTVFSnwKKLKLFVSDMIDKHREDWNPDEPRDFIDaYLKEM-----AKYPDPTT 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 289 ALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP 368
Cdd:cd20662  220 SFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGN 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 369 -VAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSK----KNKDNidpyiYTPFGSGPRNCI 443
Cdd:cd20662  300 iIPLNVPREVAVDTKLAGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLEngqfKKREA-----FLPFSMGKRACL 374
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 608788355 444 GMRFALVNMKLALVRVLQNFSFKPCKETQIPLKLRFG 480
Cdd:cd20662  375 GEQLARSELFIFFTSLLQKFTFKPPPNEKLSLKFRMG 411
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
39-467 8.07e-31

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 125.62  E-value: 8.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGN------ALSFRkgywtFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKE-----------CYSV 101
Cdd:PLN02394  33 PGPAAVPIFGNwlqvgdDLNHR-----NLAEMAKKYGDVFLLRMGQRNLVVVSSPELAKEVLHTQgvefgsrtrnvVFDI 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 102 FTnrrpfgpvGFMKNAISIAEDEEWKRIRSLLS-PTFTSGKLKEMVPIIAQYGDVLVRNLRREAET-GKPVTLKHVFGAY 179
Cdd:PLN02394 108 FT--------GKGQDMVFTVYGDHWRKMRRIMTvPFFTNKVVQQYRYGWEEEADLVVEDVRANPEAaTEGVVIRRRLQLM 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 180 SMDVITSTSFGVSIDSLNNPQdpFVentkKLLRFNP-----LDPFVLSIKVF-PFLTPILEA-LNItvfprkvisfltks 252
Cdd:PLN02394 180 MYNIMYRMMFDRRFESEDDPL--FL----KLKALNGersrlAQSFEYNYGDFiPILRPFLRGyLKI-------------- 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 253 VKQIKEGRLKETQKHRVD-FLQLMidSQNSKDSETHKALSDLELMAQ--------SIIFIF-----AGYETTSSVLSFII 318
Cdd:PLN02394 240 CQDVKERRLALFKDYFVDeRKKLM--SAKGMDKEGLKCAIDHILEAQkkgeinedNVLYIVeninvAAIETTLWSIEWGI 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 319 YELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRL-FPVAMRLERVCKKDVEINGMFIPKGVVVMIP 397
Cdd:PLN02394 318 AELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLhMAIPLLVPHMNLEDAKLGGYDIPAESKILVN 397
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 608788355 398 SYVLHHDPKYWTEPEKFLPERF---SKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:PLN02394 398 AWWLANNPELWKNPEEFRPERFleeEAKVEANGNDFRFLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLP 470
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
39-467 3.43e-30

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 123.78  E-value: 3.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGNALSFRK-GYWTFDMECyKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNR------------ 105
Cdd:PLN03112  35 PGPPRWPIVGNLLQLGPlPHRDLASLC-KKYGPLVYLRLGSVDAITTDDPELIREILLRQ-DDVFASRprtlaavhlayg 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 106 ------RPFGPvgfmknaisiaedeEWKRIRSL-LSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGA 178
Cdd:PLN03112 113 cgdvalAPLGP--------------HWKRMRRIcMEHLLTTKRLESFAKHRAEEARHLIQDVWEAAQTGKPVNLREVLGA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 179 YSMDVIT-----STSFGVSIDSLNNPQDpFVENTKKLLRFNPLdpfvlsIKVFPFLtPILEALNITVFPRK-------VI 246
Cdd:PLN03112 179 FSMNNVTrmllgKQYFGAESAGPKEAME-FMHITHELFRLLGV------IYLGDYL-PAWRWLDPYGCEKKmrevekrVD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 247 SFLTKSVKQIKEGRL-KETQKHRVDFLQLMIDSQnSKDSETHkaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHP 325
Cdd:PLN03112 251 EFHDKIIDEHRRARSgKLPGGKDMDFVDVLLSLP-GENGKEH--MDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNP 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 326 DVQQKVQKEIDTVL-PNKAPPTYDTVlQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHH 403
Cdd:PLN03112 328 RVLRKIQEELDSVVgRNRMVQESDLV-HLNYLRCVVRETFRMHPAGpFLIPHESLRATTINGYYIPAKTRVFINTHGLGR 406
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 404 DPKYWTEPEKFLPERFSKKNKDNI----DP-YIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:PLN03112 407 NTKIWDDVEEFRPERHWPAEGSRVeishGPdFKILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSP 475
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
106-467 6.10e-30

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: 121.84  E-value: 6.10e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 106 RPFGPV---GFMKNAISIAEDEEWKRIRSLLSPT---FTSGKlKEMVPIIAQYGDVLVRNLrrEAETGKPVTLKHVFGAY 179
Cdd:cd20664   37 RPIIPIfedFNKGYGILFSNGENWKEMRRFTLTTlrdFGMGK-KTSEDKILEEIPYLIEVF--EKHKGKPFETTLSMNVA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 180 SMDVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPlDPFVLSIKVFPFLTPILEALNitvfprKVISFLTKSVKQIKEG 259
Cdd:cd20664  114 VSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTG-SPSVQLYNMFPWLGPFPGDIN------KLLRNTKELNDFLMET 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 260 RLKETQKHRVDFLQLMIDS---QNSKDSETHKALSDLELMAQSIIFIF-AGYETTSSVLSFIIYELATHPDVQQKVQKEI 335
Cdd:cd20664  187 FMKHLDVLEPNDQRGFIDAflvKQQEEEESSDSFFHDDNLTCSVGNLFgAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEI 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 336 DTVLPNKAPPTYDTVlQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVmIP--SYVLhHDPKYWTEPE 412
Cdd:cd20664  267 DRVIGSRQPQVEHRK-NMPYTDAVIHEIQRFANIVpMNLPHATTRDVTFRGYFIPKGTYV-IPllTSVL-QDKTEWEKPE 343
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 608788355 413 KFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd20664  344 EFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP 398
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
243-466 1.91e-29

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: 120.60  E-value: 1.91e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 243 RKVISFLTKSVKQIKEGRLKetQKHRVDFLQLMIdSQNSKDSETHKaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELA 322
Cdd:cd20657  181 KRFDALLTKILEEHKATAQE--RKGKPDFLDFVL-LENDDNGEGER-LTDTNIKALLLNLFTAGTDTSSSTVEWALAELI 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 323 THPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVCKKDVEINGMFIPKGVVVMIPSYVL 401
Cdd:cd20657  257 RHPDILKKAQEEMDQVIGRDRRLLESDIPNLPYLQAICKETFRLHPsTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAI 336
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 402 HHDPKYWTEPEKFLPERFSKKNKDNIDP----YIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20657  337 GRDPDVWENPLEFKPERFLPGRNAKVDVrgndFELIPFGAGRRICAGTRMGIRMVEYILATLVHSFDWK 405
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
124-489 6.84e-29

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: 118.66  E-value: 6.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 124 EEWKRIRSLLSPTFTSGK-LKEMVPIIAQYGDVLVRNLRREAE---TGKPVT-LKHVFGAYSMDVITSTSFGVSIDSLNN 198
Cdd:cd20643   64 EAWRKDRLILNKEVLAPKvIDNFVPLLNEVSQDFVSRLHKRIKksgSGKWTAdLSNDLFRFALESICNVLYGERLGLLQD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 199 PQDP----FVENTKKLLRFNPldPFVlsikvfpFLTP-ILEALNITVFPRKVIS----------FLTKSVKQIKEGRlKE 263
Cdd:cd20643  144 YVNPeaqrFIDAITLMFHTTS--PML-------YIPPdLLRLINTKIWRDHVEAwdvifnhadkCIQNIYRDLRQKG-KN 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 264 TQKHRVDFLQLMIDSQNSkdSETHKAlSDLELMAqsiififAGYETTSSVLSFIIYELATHPDVQQKVQKEidtVLPNKA 343
Cdd:cd20643  214 EHEYPGILANLLLQDKLP--IEDIKA-SVTELMA-------GGVDTTSMTLQWTLYELARNPNVQEMLRAE---VLAARQ 280
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 344 PPTYDTVLQLEYLDMV---VNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS 420
Cdd:cd20643  281 EAQGDMVKMLKSVPLLkaaIKETLRLHPVAVSLQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWL 360
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 421 KKnkdNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKpcKETQIPLKLRFGGLLLTEKPI 489
Cdd:cd20643  361 SK---DITHFRNLGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIE--TQRLVEVKTTFDLILVPEKPI 424
PLN02183 PLN02183
ferulate 5-hydroxylase
39-466 9.92e-29

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 119.57  E-value: 9.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGNALSFRKGYWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVL-VKEcySVFTNRRPFGPVGFM--- 114
Cdd:PLN02183  39 PGPKGLPIIGNMLMMDQLTHRGLANLAKQYGGLFHMRMGYLHMVAVSSPEVARQVLqVQD--SVFSNRPANIAISYLtyd 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 115 KNAISIAE-DEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLrrEAETGKPVTLKHVFGAYSMDVITSTSFGvsi 193
Cdd:PLN02183 117 RADMAFAHyGPFWRQMRKLCVMKLFSRKRAESWASVRDEVDSMVRSV--SSNIGKPVNIGELIFTLTRNITYRAAFG--- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 194 DSLNNPQDPFV----ENTKKLLRFNPLD--PFVLSIKVFPFLTPILEALN-ITVFPRKVI-SFLTKSVKQIKEGRLKETQ 265
Cdd:PLN02183 192 SSSNEGQDEFIkilqEFSKLFGAFNVADfiPWLGWIDPQGLNKRLVKARKsLDGFIDDIIdDHIQKRKNQNADNDSEEAE 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 266 KHRVDFLqLMIDSQNSKDSETHKALSDLELMAQSIIFI-----FAGYETTSSVLSFIIYELATHPDVQQKVQKE-IDTVL 339
Cdd:PLN02183 272 TDMVDDL-LAFYSEEAKVNESDDLQNSIKLTRDNIKAIimdvmFGGTETVASAIEWAMAELMKSPEDLKRVQQElADVVG 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 340 PNKAPPTYDtVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF 419
Cdd:PLN02183 351 LNRRVEESD-LEKLTYLKCTLKETLRLHPPIPLLLHETAEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRF 429
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 608788355 420 SKKNKDNI--DPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:PLN02183 430 LKPGVPDFkgSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWE 478
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
113-465 9.28e-28

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 116.80  E-value: 9.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 113 FMKNAISIAEDEEWKRIRSLLSPTFTSGKLKEMVPII-AQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGV 191
Cdd:PLN03195 110 LLGDGIFNVDGELWRKQRKTASFEFASKNLRDFSTVVfREYSLKLSSILSQASFANQVVDMQDLFMRMTLDSICKVGFGV 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 192 SIDSL--NNPQDPFVE-----NTKKLLRFnpLDPFvlsikvfpflTPILEALNI---TVFPR--KVISFLTKSVKQIKEG 259
Cdd:PLN03195 190 EIGTLspSLPENPFAQafdtaNIIVTLRF--IDPL----------WKLKKFLNIgseALLSKsiKVVDDFTYSVIRRRKA 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 260 RLKETQKHRVD-----FLQLMIDSQNSKDSETHKALSDLELMaqsiiFIFAGYETTSSVLSFIIYELATHPDVQQKVQKE 334
Cdd:PLN03195 258 EMDEARKSGKKvkhdiLSRFIELGEDPDSNFTDKSLRDIVLN-----FVIAGRDTTATTLSWFVYMIMMNPHVAEKLYSE 332
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 335 I---DTVLPNKAPP-----------------TYDTVLQLEYLDMVVNETLRLFP-VAMRLERVCKKDVEINGMFIPKGVV 393
Cdd:PLN03195 333 LkalEKERAKEEDPedsqsfnqrvtqfagllTYDSLGKLQYLHAVITETLRLYPaVPQDPKGILEDDVLPDGTKVKAGGM 412
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 608788355 394 VMIPSYVLHHDPKYW-TEPEKFLPERFSKKNK-DNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:PLN03195 413 VTYVPYSMGRMEYNWgPDAASFKPERWIKDGVfQNASPFKFTAFQAGPRICLGKDSAYLQMKMALALLCRFFKF 486
PLN02687 PLN02687
flavonoid 3'-monooxygenase
243-496 1.27e-27

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 116.45  E-value: 1.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 243 RKVISFLTKSVKQIKEGRLKETQKHrVDFLQLMID--SQNSKDSETHKaLSDLELMAQSIIFIFAGYETTSSVLSFIIYE 320
Cdd:PLN02687 246 RRFDAMMNGIIEEHKAAGQTGSEEH-KDLLSTLLAlkREQQADGEGGR-ITDTEIKALLLNLFTAGTDTTSSTVEWAIAE 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 321 LATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVCKKDVEINGMFIPKGVVVMIPSY 399
Cdd:PLN02687 324 LIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHPsTPLSLPRMAAEECEINGYHIPKGATLLVNVW 403
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 400 VLHHDPKYWTEPEKFLPERF-SKKNKDNID----PYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKpCKETQIP 474
Cdd:PLN02687 404 AIARDPEQWPDPLEFRPDRFlPGGEHAGVDvkgsDFELIPFGAGRRICAGLSWGLRMVTLLTATLVHAFDWE-LADGQTP 482
                        250       260
                 ....*....|....*....|....*.
gi 608788355 475 LKLR----FGGLLLTEKPIVLKAESR 496
Cdd:PLN02687 483 DKLNmeeaYGLTLQRAVPLMVHPRPR 508
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
251-467 2.13e-27

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: 114.49  E-value: 2.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 251 KSVKQIKEGRLKETQKHRVDfLQLMIDSQNSKDSETHKALSDLELMAQ--------SIIFIF-----AGYETTSSVLSFI 317
Cdd:cd11074  178 KICKEVKERRLQLFKDYFVD-ERKKLGSTKSTKNEGLKCAIDHILDAQkkgeinedNVLYIVeninvAAIETTLWSIEWG 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 318 IYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRL-FPVAMRLERVCKKDVEINGMFIPKGVVVMI 396
Cdd:cd11074  257 IAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLrMAIPLLVPHMNLHDAKLGGYDIPAESKILV 336
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 608788355 397 PSYVLHHDPKYWTEPEKFLPERF---SKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd11074  337 NAWWLANNPAHWKKPEEFRPERFleeESKVEANGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNFELLP 410
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
123-474 3.67e-27

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: 113.95  E-value: 3.67e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 123 DEEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGK-PVTLKHVFGAYSMDVITSTSFGVSIDslNNPQD 201
Cdd:cd11066   61 DESCKRRRKAAASALNRPAVQSYAPIIDLESKSFIRELLRDSAEGKgDIDPLIYFQRFSLNLSLTLNYGIRLD--CVDDD 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 202 PF------VENtkKLLRF-----NPLDpFVLSIKVFPFLT-PILEALNITvfpRKVISFLTKSVKQIKEGRLKETQKHrv 269
Cdd:cd11066  139 SLlleiieVES--AISKFrstssNLQD-YIPILRYFPKMSkFRERADEYR---NRRDKYLKKLLAKLKEEIEDGTDKP-- 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 270 dflqlMIDSQNSKDSEThkALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHP--DVQQKVQKEIDTVLPNKAPPTY 347
Cdd:cd11066  211 -----CIVGNILKDKES--KLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPgqEIQEKAYEEILEAYGNDEDAWE 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 348 DTVL--QLEYLDMVVNETLRLFPV-AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNK 424
Cdd:cd11066  284 DCAAeeKCPYVVALVKETLRYFTVlPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASG 363
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 608788355 425 DNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIP 474
Cdd:cd11066  364 DLIPGPPHFSFGAGSRMCAGSHLANRELYTAICRLILLFRIGPKDEEEPM 413
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
218-467 3.71e-27

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: 113.74  E-value: 3.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 218 PFVLSIKVFPFLTPILEalnitvfPRKVISFLTKSVKQIKEGRLKETQKHRV-DFLQLMIDS---QNSKDSETHKALSDL 293
Cdd:cd20671  150 PGLQLFNLYPVLGAFLK-------LHKPILDKVEEVCMILRTLIEARRPTIDgNPLHSYIEAliqKQEEDDPKETLFHDA 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRL 373
Cdd:cd20671  223 NVLACTLDLVMAGTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHV 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 374 ERVCKKDVEINGMFIPKGVVVmIP--SYVLhHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVN 451
Cdd:cd20671  303 PRCTAADTQFKGYLIPKGTPV-IPllSSVL-LDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTE 380
                        250
                 ....*....|....*.
gi 608788355 452 MKLALVRVLQNFSFKP 467
Cdd:cd20671  381 LFIFFTGLLQKFTFLP 396
PLN02655 PLN02655
ent-kaurene oxidase
38-466 4.21e-27

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 114.07  E-value: 4.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  38 IPGptpLPFLGNALSF--RKGYWTFdMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSVFTNRRP--FGPVGF 113
Cdd:PLN02655   4 VPG---LPVIGNLLQLkeKKPHRTF-TKWSEIYGPIYTIRTGASSVVVLNSTEVAKEAMVTKFSSISTRKLSkaLTVLTR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 114 MKNAISIAE-DEEWKRIRSLLsptftsgkLKEMVPIIAQ-----YGDVLVRN----LRREAET--GKPVTLKHVFGAYSM 181
Cdd:PLN02655  80 DKSMVATSDyGDFHKMVKRYV--------MNNLLGANAQkrfrdTRDMLIENmlsgLHALVKDdpHSPVNFRDVFENELF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 182 DVITSTSFGVSIDSLNNPQDPFVENTKKLLRFNPLDPFVLSIKV-----FPFLTPI----LEALNITV-FPRKVI--SFL 249
Cdd:PLN02655 152 GLSLIQALGEDVESVYVEELGTEISKEEIFDVLVHDMMMCAIEVdwrdfFPYLSWIpnksFETRVQTTeFRRTAVmkALI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 250 TKSVKQIKEGrlkETQKHRVDFLQlmidsqnskDSETHkaLSDLELM---AQSIIfifAGYETTSSVLSFIIYELATHPD 326
Cdd:PLN02655 232 KQQKKRIARG---EERDCYLDFLL---------SEATH--LTDEQLMmlvWEPII---EAADTTLVTTEWAMYELAKNPD 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 327 VQQKVQKEIDTVLPNKAPpTYDTVLQLEYLDMVVNETLRLF-PVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDP 405
Cdd:PLN02655 295 KQERLYREIREVCGDERV-TEEDLPNLPYLNAVFHETLRKYsPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDK 373
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 608788355 406 KYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:PLN02655 374 KRWENPEEWDPERFLGEKYESADMYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEWR 434
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
68-467 7.51e-27

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: 112.93  E-value: 7.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKECySVFTNRRPFgPV--GFMK-NAISIAEDEEWKRIRSLLSPT---FTSGK 141
Cdd:cd20669    1 YGSVYTVYLGPRPVVVLCGYQAVKEALVDQA-EEFSGRGDY-PVffNFTKgNGIAFSNGERWKILRRFALQTlrnFGMGK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 lKEMVPIIAQYGDVLVRNLRreAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnpqdpfveNTKKLLR----FNplD 217
Cdd:cd20669   79 -RSIEERILEEAQFLLEELR--KTKGAPFDPTFLLSRAVSNIICSVVFGSRFDY----------DDKRLLTilnlIN--D 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 218 PF-VLS------IKVFPFLTPILEALNITVFP--RKVISFLTKSVKQIKEGRLKETQKHRVD-FLQLMidSQNSKDSETH 287
Cdd:cd20669  144 NFqIMSspwgelYNIFPSVMDWLPGPHQRIFQnfEKLRDFIAESVREHQESLDPNSPRDFIDcFLTKM--AEEKQDPLSH 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 288 KALSDLeLMAQSIIFiFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLF 367
Cdd:cd20669  222 FNMETL-VMTTHNLL-FGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFA 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 368 PV-AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMR 446
Cdd:cd20669  300 DIiPMSLPHAVTRDTNFRGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGES 379
                        410       420
                 ....*....|....*....|.
gi 608788355 447 FALVNMKLALVRVLQNFSFKP 467
Cdd:cd20669  380 LARMELFLYLTAILQNFSLQP 400
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
68-467 9.51e-27

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: 112.71  E-value: 9.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKECySVFTNRRPFGPV--GFMKNAISIAEDEEWKRIRSLLSPT---FTSGK- 141
Cdd:cd20670    1 YGPVFTVYMGPRPVVVLCGHEAVKEALVDQA-DEFSGRGELATIerNFQGHGVALANGERWRILRRFSLTIlrnFGMGKr 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 -LKEMVPIIAQYgdvLVRNLRREaeTGKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnpQDPFVENTKKLLRFNPLDPFV 220
Cdd:cd20670   80 sIEERIQEEAGY---LLEEFRKT--KGAPIDPTFFLSRTVSNVISSVVFGSRFDY----EDKQFLSLLRMINESFIEMST 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 221 LSIKVFPFLTPILEalnitVFPRK--VISFLTKSVKQIKEGRLKETQ-----KHRVDFLQLMIDSQNSKDSETHKALSDL 293
Cdd:cd20670  151 PWAQLYDMYSGIMQ-----YLPGRhnRIYYLIEELKDFIASRVKINEasldpQNPRDFIDCFLIKMHQDKNNPHTEFNLK 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL-PNKAPPTYDTVlQLEYLDMVVNETLRLFP-VAM 371
Cdd:cd20670  226 NLVLTTLNLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIgPHRLPSVDDRV-KMPYTDAVIHEIQRLTDiVPL 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 372 RLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVN 451
Cdd:cd20670  305 GVPHNVIRDTQFRGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARME 384
                        410
                 ....*....|....*.
gi 608788355 452 MKLALVRVLQNFSFKP 467
Cdd:cd20670  385 LFLYFTSILQNFSLRS 400
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
167-472 9.72e-27

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: 112.58  E-value: 9.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 167 GKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQDP-------FVENTKKLLRFNPLDPFVLSIKvfpFLTPILEALNIT 239
Cdd:cd20656  108 GKPVVLRKYLSAVAFNNITRLAFGKRFVNAEGVMDEqgvefkaIVSNGLKLGASLTMAEHIPWLR---WMFPLSEKAFAK 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 240 VFPRKviSFLTKSVKQIKEGRLKE--TQKHRVDFLQLMIDsqnskdsetHKALSDLELMAQSIIFIFAGYETTSSVLSFI 317
Cdd:cd20656  185 HGARR--DRLTKAIMEEHTLARQKsgGGQQHFVALLTLKE---------QYDLSEDTVIGLLWDMITAGMDTTAISVEWA 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 318 IYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVCKKDVEINGMFIPKGVVVMI 396
Cdd:cd20656  254 MAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPpTPLMLPHKASENVKIGGYDIPKGANVHV 333
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 608788355 397 PSYVLHHDPKYWTEPEKFLPERFSKKNKD-NIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQ 472
Cdd:cd20656  334 NVWAIARDPAVWKNPLEFRPERFLEEDVDiKGHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPEGTP 410
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
80-488 1.14e-26

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: 112.50  E-value: 1.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  80 PMLAITDPDMIKTVLVKECYSvFTNRRPFGPVGFMKNAISIAEDEE----WKRIRSLLSP---TFT---------SGKLK 143
Cdd:cd20677   13 PVVVVSGLETIKQVLLKQGES-FAGRPDFYTFSLIANGKSMTFSEKygesWKLHKKIAKNalrTFSkeeaksstcSCLLE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 144 EMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAysmDVITSTSFGVSIDSLNNPQDPFVENTKKLLR----FNPLDpF 219
Cdd:cd20677   92 EHVCAEASELVKTLVELSKEKGSFDPVSLITCAVA---NVVCALCFGKRYDHSDKEFLTIVEINNDLLKasgaGNLAD-F 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 220 VLSIKVFPFltPILEALNitVFPRKVISFLTKSVKQIKEGRLKETQKHRVDFLQLMIDSQNSKDSetHKALSDLELMAqS 299
Cdd:cd20677  168 IPILRYLPS--PSLKALR--KFISRLNNFIAKSVQDHYATYDKNHIRDITDALIALCQERKAEDK--SAVLSDEQIIS-T 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 300 IIFIF-AGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVC 377
Cdd:cd20677  241 VNDIFgAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHSSfVPFTIPHCT 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 378 KKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERF----SKKNKDNIDPYIYtpFGSGPRNCIGMRFALVNMK 453
Cdd:cd20677  321 TADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFldenGQLNKSLVEKVLI--FGMGVRKCLGEDVARNEIF 398
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 608788355 454 LALVRVLQNFSFKPCKETQIPLKLRFGgllLTEKP 488
Cdd:cd20677  399 VFLTTILQQLKLEKPPGQKLDLTPVYG---LTMKP 430
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
124-470 1.41e-26

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: 111.61  E-value: 1.41e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 124 EEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHV--FGAYSMDVITSTSFGvsidslnnpqD 201
Cdd:cd20615   58 TDWKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGDGRRFVIDPAqaLKFLPFRVIAEILYG----------E 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 202 PFVENTKKLLRFNPLD----PFVLSIKVFPFltpilealnitvfprKVISFLTKSVKQikegRLKETQKHRVDFLQLMID 277
Cdd:cd20615  128 LSPEEKEELWDLAPLReelfKYVIKGGLYRF---------------KISRYLPTAANR----RLREFQTRWRAFNLKIYN 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 278 S-QNSKDSETHKALSD--------LELMAQSII-FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTY 347
Cdd:cd20615  189 RaRQRGQSTPIVKLYEavekgditFEELLQTLDeMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPME 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 348 DTVL-QLEYLDMVVNETLRLFPVAM-RLERVCKKDVEINGMFIPKGVVVMIPSYVLHHD-PKYWTEPEKFLPERFSkknk 424
Cdd:cd20615  269 DYILsTDTLLAYCVLESLRLRPLLAfSVPESSPTDKIIGGYRIPANTPVVVDTYALNINnPFWGPDGEAYRPERFL---- 344
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 608788355 425 dNIDP----YIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKE 470
Cdd:cd20615  345 -GISPtdlrYNFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPDQ 393
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
124-496 5.96e-26

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: 110.53  E-value: 5.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 124 EEWKRIRSLLSPTFTSGK-LKEMVPIIAQYGDVLVR---NLRREAETGKPVTLKHVFGAYSMDVITSTSFG------VSI 193
Cdd:cd20658   59 EQWKKMRKVLTTELMSPKrHQWLHGKRTEEADNLVAyvyNMCKKSNGGGLVNVRDAARHYCGNVIRKLMFGtryfgkGME 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 194 DSLNNPQDpfVENTKKLlrFNPLD---PFVLSiKVFPFLT---------PILEALNITVFPRKVIsfLTKSVKQIKEGRL 261
Cdd:cd20658  139 DGGPGLEE--VEHMDAI--FTALKclyAFSIS-DYLPFLRgldldghekIVREAMRIIRKYHDPI--IDERIKQWREGKK 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 262 KETQkhrvDFLQLMIdsqNSKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPN 341
Cdd:cd20658  212 KEEE----DWLDVFI---TLKDENGNPLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGK 284
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 342 KAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS 420
Cdd:cd20658  285 ERLVQESDIPNLNYVKACAREAFRLHPVApFNVPHVAMSDTTVGGYFIPKGSHVLLSRYGLGRNPKVWDDPLKFKPERHL 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 421 KKNKDNI--DPYI-YTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK-PCKETQIPLKLRFGGLLLTeKPIVLKAESR 496
Cdd:cd20658  365 NEDSEVTltEPDLrFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTlPPNVSSVDLSESKDDLFMA-KPLVLVAKPR 443
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
262-462 8.79e-25

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: 106.82  E-value: 8.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 262 KETQKHRVDFLQLMIDsQNSKDSEthkALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPN 341
Cdd:cd20638  202 EDTEQQCKDALQLLIE-HSRRNGE---PLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLL 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 342 KAPPTYDTVL------QLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFL 415
Cdd:cd20638  278 STKPNENKELsmevleQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVADIFPNKDEFN 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 608788355 416 PERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQN 462
Cdd:cd20638  358 PDRFMSPLPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARH 404
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
294-491 2.56e-24

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: 105.31  E-value: 2.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 294 ELMAqsiififAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVlPNKAPPTYDTVLQ-LEYLDMVVNETLRLFPVAMR 372
Cdd:cd20644  239 ELTA-------GGVDTTAFPLLFTLFELARNPDVQQILRQESLAA-AAQISEHPQKALTeLPLLKAALKETLRLYPVGIT 310
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 373 LERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKnKDNIDPYIYTPFGSGPRNCIGMRFALVNM 452
Cdd:cd20644  311 VQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDI-RGSGRNFKHLAFGFGMRQCLGRRLAEAEM 389
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 608788355 453 KLALVRVLQNFSFKPCkeTQIPLKLRFGGLLLTEKPIVL 491
Cdd:cd20644  390 LLLLMHVLKNFLVETL--SQEDIKTVYSFILRPEKPPLL 426
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
251-467 2.71e-24

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: 105.13  E-value: 2.71e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 251 KSVKQIKE--GRLKETQKHRV----------DFLQLMIDSQNskdsetHKALSdLELMAQSII-FIFAGYETTSSVLSFI 317
Cdd:cd20616  175 KAVKDLKDaiEILIEQKRRRIstaekledhmDFATELIFAQK------RGELT-AENVNQCVLeMLIAAPDTMSVSLFFM 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 318 IYELATHPDVQQKVQKEIDTVLPNKAPpTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIP 397
Cdd:cd20616  248 LLLIAQHPEVEEAILKEIQTVLGERDI-QNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKGTNIILN 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 608788355 398 SYVLHHDPkYWTEPEKFLPERFSKKNkdnidPYIY-TPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd20616  327 IGRMHRLE-FFPKPNEFTLENFEKNV-----PSRYfQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCT 391
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
248-466 2.79e-24

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: 105.26  E-value: 2.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 248 FLTKSVKQIKEGRLKETQKHRVD-FLQLMIDSQNSKDSETHKAlsdlELMAQSIIFIFAGYETTSSVLSFIIYELATHPD 326
Cdd:cd20668  183 FIAKKVEHNQRTLDPNSPRDFIDsFLIRMQEEKKNPNTEFYMK----NLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPE 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 327 VQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVV--MIPSyvLHH 403
Cdd:cd20668  259 VEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIpMGLARRVTKDTKFRDFFLPKGTEVfpMLGS--VLK 336
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 608788355 404 DPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20668  337 DPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRFK 399
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
249-467 3.93e-24

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 104.65  E-value: 3.93e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 249 LTKSVKQIKEGRLKETQKHR-----------VD-FLQLMIDSQNSKDSETHkalsdLELMAQSIIFIF-AGYETTSSVLS 315
Cdd:cd20665  173 LLKNVAYIKSYILEKVKEHQesldvnnprdfIDcFLIKMEQEKHNQQSEFT-----LENLAVTVTDLFgAGTETTSTTLR 247
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 316 FIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLR---LFPvaMRLERVCKKDVEINGMFIPKGV 392
Cdd:cd20665  248 YGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRyidLVP--NNLPHAVTCDTKFRNYLIPKGT 325
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 608788355 393 VVMIP-SYVLhHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd20665  326 TVITSlTSVL-HDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKS 400
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
243-493 6.72e-24

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 104.93  E-value: 6.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 243 RKVISFLTKSVKQikEGRLKETQKHRVDFLQLMIDSQNSKDSEThkaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELA 322
Cdd:PLN00110 243 KKFDKLLTRMIEE--HTASAHERKGNPDFLDVVMANQENSTGEK---LTLTNIKALLLNLFTAGTDTSSSVIEWSLAEML 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 323 THPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVCKKDVEINGMFIPKGVVVMIPSYVL 401
Cdd:PLN00110 318 KNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKESFRKHPsTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAI 397
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 402 HHDPKYWTEPEKFLPERFSKKNKDNIDP----YIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQIPLKL 477
Cdd:PLN00110 398 GRDPDVWENPEEFRPERFLSEKNAKIDPrgndFELIPFGAGRRICAGTRMGIVLVEYILGTLVHSFDWKLPDGVELNMDE 477
                        250
                 ....*....|....*.
gi 608788355 478 RFGglLLTEKPIVLKA 493
Cdd:PLN00110 478 AFG--LALQKAVPLSA 491
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
198-483 8.66e-24

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: 103.77  E-value: 8.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 198 NPQDPFVENTKKLL-------RFNPLDPFVLSI-------------------KVFPFLTPILEALNITVFPRK--VISFL 249
Cdd:cd20667  105 DPQDPIVHATANVIgavvfghRFSSEDPIFLELirainlglafastiwgrlyDAFPWLMRYLPGPHQKIFAYHdaVRSFI 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 250 TKSVkQIKEGRLKETQKHRVDFLQlmidSQNSKDSETHKALSDLELMAQSIIFIF-AGYETTSSVLSFIIYELATHPDVQ 328
Cdd:cd20667  185 KKEV-IRHELRTNEAPQDFIDCYL----AQITKTKDDPVSTFSEENMIQVVIDLFlGGTETTATTLHWALLYMVHHPEIQ 259
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 329 QKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPV-AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKY 407
Cdd:cd20667  260 EKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVvSVGAVRQCVTSTTMHGYYVEKGTIILPNLASVLYDPEC 339
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 608788355 408 WTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK-PCKETQIPLKLRFGGLL 483
Cdd:cd20667  340 WETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNFQlPEGVQELNLEYVFGGTL 416
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
305-465 1.71e-23

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: 102.85  E-value: 1.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 305 AGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEI 383
Cdd:cd20663  241 AGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVpLGVPHMTSRDIEV 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 384 NGMFIPKGVVVMIP-SYVLhHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQN 462
Cdd:cd20663  321 QGFLIPKGTTLITNlSSVL-KDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQR 399

                 ...
gi 608788355 463 FSF 465
Cdd:cd20663  400 FSF 402
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
68-464 2.11e-23

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: 102.55  E-value: 2.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  68 YRKVWGIYDCQQPMLAITDPDMIKTVLVKECySVFTNRRPFG---PVgFMKNAISIAEDEEWKRIRSLLSPT---FTSGK 141
Cdd:cd20672    1 YGDVFTVHLGPRPVVMLCGTDAIREALVDQA-EAFSGRGTIAvvdPI-FQGYGVIFANGERWKTLRRFSLATmrdFGMGK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 lKEMVPIIAQYGDVLVRNLRREaeTGKPVTLKHVFGAYSMDVITSTSFGVSIDSlnnpQDPfventkKLLRFnpLDPFV- 220
Cdd:cd20672   79 -RSVEERIQEEAQCLVEELRKS--KGALLDPTFLFQSITANIICSIVFGERFDY----KDP------QFLRL--LDLFYq 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 221 -------LSIKVFPFLTPILEalnitVFP---RKVisflTKSVKQIKEGRLKETQKHRV--------DFLQLMIDSQNSK 282
Cdd:cd20672  144 tfslissFSSQVFELFSGFLK-----YFPgahRQI----YKNLQEILDYIGHSVEKHRAtldpsaprDFIDTYLLRMEKE 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 283 DSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNE 362
Cdd:cd20672  215 KSNHHTEFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHE 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 363 TLRLFPVA-MRLERVCKKDVEINGMFIPKGV-VVMIPSYVLhHDPKYWTEPEKFLPERFSKKNKDNIDPYIYTPFGSGPR 440
Cdd:cd20672  295 IQRFSDLIpIGVPHRVTKDTLFRGYLLPKNTeVYPILSSAL-HDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKR 373
                        410       420
                 ....*....|....*....|....
gi 608788355 441 NCIGMRFALVNMKLALVRVLQNFS 464
Cdd:cd20672  374 ICLGEGIARNELFLFFTTILQNFS 397
PLN02302 PLN02302
ent-kaurenoic acid oxidase
39-474 2.14e-23

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 103.25  E-value: 2.14e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGNALSFRKGYWTFDMECY-----KKYRKVwGIYDC---QQPMLAITDPDMIKTVLVKEcySVFTNRRPFGP 110
Cdd:PLN02302  45 PGDLGWPVIGNMWSFLRAFKSSNPDSFiasfiSRYGRT-GIYKAfmfGQPTVLVTTPEACKRVLTDD--DAFEPGWPEST 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 111 VGFM--KNAISIAEDEEwKRIRSLLSPTFTSGK-LKEMVPIIAQygdVLVRNLRREAETGKPVTLKHVfGAYSMDVITST 187
Cdd:PLN02302 122 VELIgrKSFVGITGEEH-KRLRRLTAAPVNGPEaLSTYIPYIEE---NVKSCLEKWSKMGEIEFLTEL-RKLTFKIIMYI 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 188 SFgvSIDSlnnpqDPFVENTKKLlrFNPLDPFVLSIkvfpfltpileALNITVFP--------RKVISFLTKSVKQIKEG 259
Cdd:PLN02302 197 FL--SSES-----ELVMEALERE--YTTLNYGVRAM-----------AINLPGFAyhralkarKKLVALFQSIVDERRNS 256
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 260 RLKETQKHRVDFLQLMIDSQNskdsETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL 339
Cdd:PLN02302 257 RKQNISPRKKDMLDLLLDAED----ENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEQEEIA 332
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 340 PNKAPP----TYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFL 415
Cdd:PLN02302 333 KKRPPGqkglTLKDVRKMEYLSQVIDETLRLINISLTVFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFD 412
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 608788355 416 PERFskkNKDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP----CKETQIP 474
Cdd:PLN02302 413 PSRW---DNYTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERlnpgCKVMYLP 472
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
66-460 4.86e-23

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: 101.83  E-value: 4.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  66 KKYRKVWGIYDCQQPMLAITDPDMIKTVLVKEcYSVFTNRRP------FGPvgfmkNAISIAEDEEWKRIRSLLSPTFTS 139
Cdd:cd20636   20 EKYGNVFKTHLLGRPVIRVTGAENIRKILLGE-HTLVSTQWPqstrilLGS-----NTLLNSVGELHRQRRKVLARVFSR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 140 GKLKEMVPIIAqygDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVS-----IDSLNNPQDPFVENTKKLlrfn 214
Cdd:cd20636   94 AALESYLPRIQ---DVVRSEVRGWCRGPGPVAVYTAAKSLTFRIAVRILLGLRleeqqFTYLAKTFEQLVENLFSL---- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 215 PLDpfvlsikvFPFltpilEALNITVFPRKVI-SFLTKSVKQ-IKEGRLKETQkhrvDFLQLMIDSQNSKDSEthkaLSD 292
Cdd:cd20636  167 PLD--------VPF-----SGLRKGIKARDILhEYMEKAIEEkLQRQQAAEYC----DALDYMIHSARENGKE----LTM 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 293 LELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDT--------VLPNKAppTYDTVLQLEYLDMVVNETL 364
Cdd:cd20636  226 QELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVShglidqcqCCPGAL--SLEKLSRLRYLDCVVKEVL 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 365 RLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS-KKNKDNIDPYIYTPFGSGPRNCI 443
Cdd:cd20636  304 RLLPPVSGGYRTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGvEREESKSGRFNYIPFGGGVRSCI 383
                        410
                 ....*....|....*..
gi 608788355 444 GMRFALVNMKLALVRVL 460
Cdd:cd20636  384 GKELAQVILKTLAVELV 400
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
208-497 1.14e-22

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 100.82  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 208 KKLLRFNPLD-------PFVLSIKVF---PFltPILEALNITVFP--RKVISFLTKSVKQIKEGRlKETQKHRVDFLQLM 275
Cdd:PLN02987 180 KQLMSFDPGEwteslrkEYVLVIEGFfsvPL--PLFSTTYRRAIQarTKVAEALTLVVMKRRKEE-EEGAEKKKDMLAAL 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 276 IDSQNSkdsethkaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP---TYDTVLQ 352
Cdd:PLN02987 257 LASDDG--------FSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEHEKIRAMKSDSyslEWSDYKS 328
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 353 LEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIY 432
Cdd:PLN02987 329 MPFTQCVVNETLRVANIIGGIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVF 408
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 608788355 433 TPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETqiplKLRFGGLLLTEKPIVLKAESRD 497
Cdd:PLN02987 409 TPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPAEQD----KLVFFPTTRTQKRYPINVKRRD 469
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
241-465 1.55e-22

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: 100.09  E-value: 1.55e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 241 FPRKVISFLTKSVKQIKEGRLKEtqkHRVDFLQLMID-SQNSKDSEThkalSDLELMAQSIIFIF-----AGYETTSSVL 314
Cdd:cd20676  185 INKRFNSFLQKIVKEHYQTFDKD---NIRDITDSLIEhCQDKKLDEN----ANIQLSDEKIVNIVndlfgAGFDTVTTAL 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 315 SFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLR---LFPVAmrLERVCKKDVEINGMFIPKG 391
Cdd:cd20676  258 SWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFRhssFVPFT--IPHCTTRDTSLNGYYIPKD 335
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 608788355 392 VVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYI---YTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd20676  336 TCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTEINKTEsekVMLFGLGKRRCIGESIARWEVFLFLAILLQQLEF 412
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
249-466 5.17e-22

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: 98.38  E-value: 5.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 249 LTKSVKQIKEGRLKETQ-KHRVDFLQLMIDSQNskdsETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDV 327
Cdd:cd20637  184 LQKSLEKAIREKLQGTQgKDYADALDILIESAK----EHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGV 259
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 328 QQKVQKEI--DTVLPNKAPP----TYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVL 401
Cdd:cd20637  260 LEKLREELrsNGILHNGCLCegtlRLDTISSLKYLDCVIKEVLRLFTPVSGGYRTALQTFELDGFQIPKGWSVLYSIRDT 339
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 608788355 402 HHDPKYWTEPEKFLPERFSKKNKDNID-PYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:cd20637  340 HDTAPVFKDVDAFDPDRFGQERSEDKDgRFHYLPFGGGVRTCLGKQLAKLFLKVLAVELASTSRFE 405
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
300-466 8.46e-22

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 98.61  E-value: 8.46e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 300 IIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL-PNKAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCK 378
Cdd:PLN02426 299 VSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMgPNQEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAA 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 379 K-DVEINGMFIPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSKKNK-DNIDPYIYTPFGSGPRNCIGMRFALVNMKLA 455
Cdd:PLN02426 379 EdDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPERWLKNGVfVPENPFKYPVFQAGLRVCLGKEMALMEMKSV 458
                        170
                 ....*....|.
gi 608788355 456 LVRVLQNFSFK 466
Cdd:PLN02426 459 AVAVVRRFDIE 469
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
65-464 1.40e-21

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: 96.51  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  65 YKKYRKVWGIY---DCQQpmlAITDPDMIKtvlvkecySVFTNRRPFGPVGFMKNAISIAEDEEWKRIRSLLSPTFTSGK 141
Cdd:cd11032    8 YDEETGAWHVFryaDVKR---VLSDPATFS--------SDLGRLLPGEDDALTEGSLLTMDPPRHRKLRKLVSQAFTPRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 142 LKEMVPIIAQygdvLVRNLRREAETGKPVTLKHVFgAYSMDVI-TSTSFGVsidslnNPQDpfVENTKKLLrfnplDPFV 220
Cdd:cd11032   77 IADLEPRIAE----ITDELLDAVDGRGEFDLVEDL-AYPLPVIvIAELLGV------PAED--RELFKKWS-----DALV 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 221 LSIKVFPFLTPILEALNITVfpRKVISFLTKsvkQIKEGRLKETQKHRVDFLQLMIDSQnskdsethkALSDLELMAQSI 300
Cdd:cd11032  139 SGLGDDSFEEEEVEEMAEAL--RELNAYLLE---HLEERRRNPRDDLISRLVEAEVDGE---------RLTDEEIVGFAI 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVlPNkapptydtvlqleyldmVVNETLRLFPVAMRLERVCKKD 380
Cdd:cd11032  205 LLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLI-PG-----------------AIEEVLRYRPPVQRTARVTTED 266
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 381 VEINGMFIPKG--VVVMIPSyvLHHDPKYWTEPEKFLPERfskknkdniDPYIYTPFGSGPRNCIGMRFALVNMKLALVR 458
Cdd:cd11032  267 VELGGVTIPAGqlVIAWLAS--ANRDERQFEDPDTFDIDR---------NPNPHLSFGHGIHFCLGAPLARLEARIALEA 335

                 ....*.
gi 608788355 459 VLQNFS 464
Cdd:cd11032  336 LLDRFP 341
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
313-465 7.27e-21

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: 94.68  E-value: 7.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 313 VLSFIIyelaTHPDVQQKVQKEIDTVLPN----KAPPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKdVEINGMFI 388
Cdd:cd20635  233 TLAFIL----SHPSVYKKVMEEISSVLGKagkdKIKISEDDLKKMPYIKRCVLEAIRLRSPGAITRKVVKP-IKIKNYTI 307
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 608788355 389 PKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKN-KDNIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd20635  308 PAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKADlEKNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDF 385
PLN02966 PLN02966
cytochrome P450 83A1
39-466 7.42e-21

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 95.58  E-value: 7.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGNALSFRK-GYWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSvFTNRRPFGP---VGFM 114
Cdd:PLN02966  32 PGPSPLPVIGNLLQLQKlNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVN-FADRPPHRGhefISYG 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 115 KNAISIAEDEEWKR-IRSL-LSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVS 192
Cdd:PLN02966 111 RRDMALNHYTPYYReIRKMgMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKK 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 193 IDSLNNPQDPFVentKKLLRFNPLDPFVLSIKVFPFLTPILEALNITVFPRKVISFLTKSVKQIKEGRL--KETQKHRVD 270
Cdd:PLN02966 191 YNEDGEEMKRFI---KILYGTQSVLGKIFFSDFFPYCGFLDDLSGLTAYMKECFERQDTYIQEVVNETLdpKRVKPETES 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 271 FLQLMIDSQNSKDSETHKALSDLELMAQSIIFifAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP--TYD 348
Cdd:PLN02966 268 MIDLLMEIYKEQPFASEFTVDNVKAVILDIVV--AGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTfvTED 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 349 TVLQLEYLDMVVNETLRLFPV-AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYW-TEPEKFLPERFSKKNKD- 425
Cdd:PLN02966 346 DVKNLPYFRALVKETLRIEPViPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDf 425
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 608788355 426 NIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:PLN02966 426 KGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLNFNFK 466
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
270-444 7.84e-21

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: 95.07  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 270 DFLQLMIDSQNSKDSETHKALSDLELMAQSIIFIF-AGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYD 348
Cdd:cd20675  210 DMMDAFILALEKGKSGDSGVGLDKEYVPSTVTDIFgASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIE 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 349 TVLQLEYLDMVVNETLRL--FpVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKK---- 422
Cdd:cd20675  290 DQPNLPYVMAFLYEAMRFssF-VPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDEngfl 368
                        170       180
                 ....*....|....*....|..
gi 608788355 423 NKDNIDPYIYtpFGSGPRNCIG 444
Cdd:cd20675  369 NKDLASSVMI--FSVGKRRCIG 388
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
84-467 1.40e-20

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: 93.42  E-value: 1.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  84 ITDPDMIKTVLvkECYSVFTNRRPFGP--VGFMKNAISIAED-EEWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNL 160
Cdd:cd11035   18 VTRGEDIREVL--RDPETFSSRVITVPppAGEPYPLIPLELDpPEHTRYRRLLNPLFSPKAVAALEPRIRERAVELIESF 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 161 RRE------AETGKPVTLkHVFgaysMDVitstsFGVSIDSLnnpqDPFVENTKKLLRFNPLDPFVLSI-KVFPFLTPIL 233
Cdd:cd11035   96 APRgecdfvADFAEPFPT-RVF----LEL-----MGLPLEDL----DRFLEWEDAMLRPDDAEERAAAAqAVLDYLTPLI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 234 EAlnitvfpRKvisfltksvkqikegrlketQKHRVDFLQLMIDSQnskdsETHKALSDLELMAQSIIFIFAGYETTSSV 313
Cdd:cd11035  162 AE-------RR--------------------ANPGDDLISAILNAE-----IDGRPLTDDELLGLCFLLFLAGLDTVASA 209
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 314 LSFIIYELATHPDVQQKVQKEIDTVLpnkapptydtvlqleyldMVVNETLRLFPVaMRLERVCKKDVEINGMFIPKGVV 393
Cdd:cd11035  210 LGFIFRHLARHPEDRRRLREDPELIP------------------AAVEELLRRYPL-VNVARIVTRDVEFHGVQLKAGDM 270
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 608788355 394 VMIPSYVLHHDPKYWTEPEKFLPERfskknkdniDPYIYTPFGSGPRNCIGMRFALVNMKLAL---VRVLQNFSFKP 467
Cdd:cd11035  271 VLLPLALANRDPREFPDPDTVDFDR---------KPNRHLAFGAGPHRCLGSHLARLELRIALeewLKRIPDFRLAP 338
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
283-460 2.86e-20

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: 92.96  E-value: 2.86e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 283 DSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLpNKAPPTYDTVLQLEYLDMVVNE 362
Cdd:cd20627  191 DSLLQGNLSEQQVLEDSMIFSLAGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVL-GKGPITLEKIEQLRYCQQVLCE 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 363 TLR---LFPVAMRLERVCKKdveINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNidpyIYTPFG-SG 438
Cdd:cd20627  270 TVRtakLTPVSARLQELEGK---VDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRFDDESVMK----SFSLLGfSG 342
                        170       180
                 ....*....|....*....|..
gi 608788355 439 PRNCIGMRFALVnMKLALVRVL 460
Cdd:cd20627  343 SQECPELRFAYM-VATVLLSVL 363
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
289-460 6.93e-20

cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly uncharacterized proteins including Sinorhizobium fredii CYPBJ-4 homolog. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 91.73  E-value: 6.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 289 ALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVlpNKAPPTYDTVLQLEYLDMVVNETLRLFP 368
Cdd:cd20614  203 GLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEALFRETLRLHP 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 369 VAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFsKKNKDNIDPYIYTPFGSGPRNCIGMRFA 448
Cdd:cd20614  281 PVPFVFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERW-LGRDRAPNPVELLQFGGGPHFCLGYHVA 359
                        170
                 ....*....|....*
gi 608788355 449 ---LVNMKLALVRVL 460
Cdd:cd20614  360 cveLVQFIVALAREL 374
PLN02971 PLN02971
tryptophan N-hydroxylase
150-496 3.17e-19

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 90.87  E-value: 3.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 150 AQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTSFGVSIDSLNNPQD--PFVENTKKLLRFNPLDPFVLSIKVFP 227
Cdd:PLN02971 178 AEETDHLTAWLYNMVKNSEPVDLRFVTRHYCGNAIKRLMFGTRTFSEKTEPDggPTLEDIEHMDAMFEGLGFTFAFCISD 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 228 FLtPILEALNIT---VFPRKVISFLTKSVKQIKEGRLK---ETQKHRV-DFLQLMIdsqNSKDSETHKALSDLELMAQSI 300
Cdd:PLN02971 258 YL-PMLTGLDLNgheKIMRESSAIMDKYHDPIIDERIKmwrEGKRTQIeDFLDIFI---SIKDEAGQPLLTADEIKPTIK 333
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKK 379
Cdd:PLN02971 334 ELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAaFNLPHVALS 413
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 380 DVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKD---NIDPYIYTPFGSGPRNCIGMRFALVNMKLAL 456
Cdd:PLN02971 414 DTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEvtlTENDLRFISFSTGKRGCAAPALGTAITTMML 493
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 608788355 457 VRVLQNFSFK-PCKETQIPLKLRFGGLLLTeKPIVLKAESR 496
Cdd:PLN02971 494 ARLLQGFKWKlAGSETRVELMESSHDMFLS-KPLVMVGELR 533
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
112-463 3.61e-19

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: 88.90  E-value: 3.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 112 GFMKNAISIAEDEEWKRIRSLLSPTFTSgklkEMVpiiAQYGDVLVRNLRRE-----AETGKPVTLKHVFGAYSMDVItS 186
Cdd:cd20629   42 PFLGHSILAMDGEEHRRRRRLLQPAFAP----RAV---ARWEEPIVRPIAEElvddlADLGRADLVEDFALELPARVI-Y 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 187 TSFGVsidslnnPQDPFVENTKkllrfnpldpfvLSIKVFPFLTPIlealnitvfPRKVISFLTKSVKQIKEGRLKETQ- 265
Cdd:cd20629  114 ALLGL-------PEEDLPEFTR------------LALAMLRGLSDP---------PDPDVPAAEAAAAELYDYVLPLIAe 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 266 ---KHRVDFLQLMIdsQNSKDSEThkaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKeidtvlpnk 342
Cdd:cd20629  166 rrrAPGDDLISRLL--RAEVEGEK---LDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRR--------- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 343 apptydtvlQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFlperfskk 422
Cdd:cd20629  232 ---------DRSLIPAAIEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANRDEDVYPDPDVF-------- 294
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 608788355 423 nkdNID--PYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20629  295 ---DIDrkPKPHLVFGGGAHRCLGEHLARVELREALNALLDRL 334
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
318-467 7.10e-19

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: 88.96  E-value: 7.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 318 IYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVL-----QLEYLDMVVNETLRLfPVAMRLERVCKKD-VEINGMFIPKG 391
Cdd:cd11040  247 LAHILSDPELLERIREEIEPAVTPDSGTNAILDLtdlltSCPLLDSTYLETLRL-HSSSTSVRLVTEDtVLGGGYLLRKG 325
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 392 VVVMIPSYVLHHDPKYW-TEPEKFLPERFSKKNKD---NIDPYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKP 467
Cdd:cd11040  326 SLVMIPPRLLHMDPEIWgPDPEEFDPERFLKKDGDkkgRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEP 405
PLN00168 PLN00168
Cytochrome P450; Provisional
39-466 7.17e-19

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 89.62  E-value: 7.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGNALSFRKGywTFDME-----CYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVkECYSVFTNRRPFGPV-- 111
Cdd:PLN00168  38 PGPPAVPLLGSLVWLTNS--SADVEpllrrLIARYGPVVSLRVGSRLSVFVADRRLAHAALV-ERGAALADRPAVASSrl 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 112 -GFMKNAISIAEDEEWKRI--RSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTS 188
Cdd:PLN00168 115 lGESDNTITRSSYGPVWRLlrRNLVAETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVLMC 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 189 FGVSIDS------LNNPQDPFVENTKKLLRFNpldpFVLSIKVFPFLTPILEALNITVFPRKVISFLTKSVKQIKE--GR 260
Cdd:PLN00168 195 FGERLDEpavraiAAAQRDWLLYVSKKMSVFA----FFPAVTKHLFRGRLQKALALRRRQKELFVPLIDARREYKNhlGQ 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 261 LKETQKHRVDFLQLMIDS--QNSKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTV 338
Cdd:PLN00168 271 GGEPPKKETTFEHSYVDTllDIRLPEDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAK 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 339 LPNKAPP-TYDTVLQLEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLP 416
Cdd:PLN00168 351 TGDDQEEvSEEDVHKMPYLKAVVLEGLRKHPPAhFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVP 430
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 608788355 417 ERF-------------SKKNKdnidpyiYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:PLN00168 431 ERFlaggdgegvdvtgSREIR-------MMPFGVGRRICAGLGIAMLHLEYFVANMVREFEWK 486
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
285-456 1.18e-18

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 88.84  E-value: 1.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 285 ETHKALSDlELMAQSII-FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPP---TYDTVLQLEYLDMVV 360
Cdd:PLN02196 255 GDKEGLTD-EQIADNIIgVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDKEEGeslTWEDTKKMPLTSRVI 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 361 NETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKdnidPYIYTPFGSGPR 440
Cdd:PLN02196 334 QETLRVASILSFTFREAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAPK----PNTFMPFGNGTH 409
                        170
                 ....*....|....*.
gi 608788355 441 NCIGMRFALVNMKLAL 456
Cdd:PLN02196 410 SCPGNELAKLEISVLI 425
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
270-463 3.26e-18

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: 86.33  E-value: 3.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 270 DFLQLMIDSQNSKDSethkaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTvLPNkapptydt 349
Cdd:cd20630  184 DLLTTLLRAEEDGER-----LSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAEPEL-LRN-------- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 350 vlqleyldmVVNETLRlFPVA--MRLERVCKKDVEINGMFIPKG--VVVMIPSYVLhhDPKYWTEPEKFLPERfskKNKD 425
Cdd:cd20630  250 ---------ALEEVLR-WDNFgkMGTARYATEDVELCGVTIRKGqmVLLLLPSALR--DEKVFSDPDRFDVRR---DPNA 314
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 608788355 426 NIdpyiytPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20630  315 NI------AFGYGPHFCIGAALARLELELAVSTLLRRF 346
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
99-460 4.74e-18

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 85.85  E-value: 4.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  99 YSVFTNRR-PFG-PVGFMKNAISIAEDE-EWKRIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRnlrREAETGkpvtlkhv 175
Cdd:cd11034   31 TDTFSSKGvTFPrPELGEFRLMPIETDPpEHKKYRKLLNPFFTPEAVEAFRPRVRQLTNDLID---AFIERG-------- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 176 fgaySMDVITSTSFGVSIDSlnnpqdpfvenTKKLLRFNPLDPFVLSIKVFPFLTPILEALNITVFPRKVISFltksVKQ 255
Cdd:cd11034  100 ----ECDLVTELANPLPARL-----------TLRLLGLPDEDGERLRDWVHAILHDEDPEEGAAAFAELFGHL----RDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 256 IKEGRlketQKHRVDFLQLMIDSQNSKdsethKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVqkeI 335
Cdd:cd11034  161 IAERR----ANPRDDLISRLIEGEIDG-----KPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHPEDRRRL---I 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 336 DtvlpnkapptydtvlQLEYLDMVVNETLRLF-PVAMrLERVCKKDVEINGMFIPKG--VVVMIPSyvLHHDPKYWTEPE 412
Cdd:cd11034  229 A---------------DPSLIPNAVEEFLRFYsPVAG-LARTVTQEVEVGGCRLKPGdrVLLAFAS--ANRDEEKFEDPD 290
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 608788355 413 KFLPERFSKKnkdnidpyiYTPFGSGPRNCIGMRFALVNMKLALVRVL 460
Cdd:cd11034  291 RIDIDRTPNR---------HLAFGSGVHRCLGSHLARVEARVALTEVL 329
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
290-463 4.86e-18

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: 86.08  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 290 LSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVlpnkaPPTydtvlqleyldmvVNETLRLFPV 369
Cdd:cd11031  202 LSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRADPELV-----PAA-------------VEELLRYIPL 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 370 --AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNkdnidpyiyTPFGSGPRNCIGMRF 447
Cdd:cd11031  264 gaGGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLDREPNPH---------LAFGHGPHHCLGAPL 334
                        170
                 ....*....|....*.
gi 608788355 448 ALVNMKLALVRVLQNF 463
Cdd:cd11031  335 ARLELQVALGALLRRL 350
PLN03018 PLN03018
homomethionine N-hydroxylase
282-496 5.47e-18

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 86.99  E-value: 5.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 282 KDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVN 361
Cdd:PLN03018 302 KDQNGKYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCR 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 362 ETLRLFPVAMRL-ERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKknKDNIDPYI--------Y 432
Cdd:PLN03018 382 ETFRIHPSAHYVpPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQ--GDGITKEVtlvetemrF 459
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 608788355 433 TPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKETQiPLKLRF-GGLLLTEKPIVLKAESR 496
Cdd:PLN03018 460 VSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNWKLHQDFG-PLSLEEdDASLLMAKPLLLSVEPR 523
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
290-456 1.11e-16

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 81.88  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 290 LSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQkeidtvlpnkAPPTYdtvlqleyLDMVVNETLRLFPV 369
Cdd:cd11078  205 LTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLR----------ADPSL--------IPNAVEETLRYDSP 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 370 AMRLERVCKKDVEINGMFIPKGVVVMipsyVLH----HDPKYWTEPEKFLPERfskknkDNIDPYIytPFGSGPRNCIGM 445
Cdd:cd11078  267 VQGLRRTATRDVEIGGVTIPAGARVL----LLFgsanRDERVFPDPDRFDIDR------PNARKHL--TFGHGIHFCLGA 334
                        170
                 ....*....|.
gi 608788355 446 RFALVNMKLAL 456
Cdd:cd11078  335 ALARMEARIAL 345
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
39-465 1.19e-16

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 82.82  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355  39 PGPTPLPFLGNALSFRK-GYWTFDMECYKKYRKVWGIYDCQQPMLAITDPDMIKTVLVKECYSvFTNRrpfgPVGFMKNA 117
Cdd:PLN03234  31 PGPKGLPIIGNLHQMEKfNPQHFLFRLSKLYGPIFTMKIGGRRLAVISSAELAKELLKTQDLN-FTAR----PLLKGQQT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 118 ISIAEDE--------EWKRIRSL-LSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKHVFGAYSMDVITSTS 188
Cdd:PLN03234 106 MSYQGRElgfgqytaYYREMRKMcMVNLFSPNRVASFRPVREEECQRMMDKIYKAADQSGTVDLSELLLSFTNCVVCRQA 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 189 FGVSIDSLNNPQDPFVE---NTKKLLR---FNPLDPFvlsikvFPFLTPI--LEALNITVFpRKVISFLTKSVKQ-IKEG 259
Cdd:PLN03234 186 FGKRYNEYGTEMKRFIDilyETQALLGtlfFSDLFPY------FGFLDNLtgLSARLKKAF-KELDTYLQELLDEtLDPN 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 260 RLKETQKHRVDFLQLMIDSQNSKDSETHKalsdlELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVL 339
Cdd:PLN03234 259 RPKQETESFIDLLMQIYKDQPFSIKFTHE-----NVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVI 333
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 340 PNKAPPTYDTVLQLEYLDMVVNETLRLFPV-AMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPE 417
Cdd:PLN03234 334 GDKGYVSEEDIPNLPYLKAVIKESLRLEPViPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWGDnPNEFIPE 413
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 608788355 418 RFSKKNKdNID----PYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNFSF 465
Cdd:PLN03234 414 RFMKEHK-GVDfkgqDFELLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFDW 464
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
128-463 8.23e-16

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: 79.13  E-value: 8.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 128 RIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAEtgkpvtlkhvfgaysMDVIT-----------STSFGVSIDSl 196
Cdd:cd20625   67 RLRRLVSKAFTPRAVERLRPRIERLVDELLDRLAARGR---------------VDLVAdfayplpvrviCELLGVPEED- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 197 nnpQDPFVENTKKLLRFnpLDPFVLSIKvfpfLTPILEALnitvfpRKVISFLTKSVKQikegRLKETQKhrvDFLQLMI 276
Cdd:cd20625  131 ---RPRFRGWSAALARA--LDPGPLLEE----LARANAAA------AELAAYFRDLIAR----RRADPGD---DLISALV 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 277 DSQNSKDsethkALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVqkeidtvlpnKAPPtydtvlqlEYL 356
Cdd:cd20625  189 AAEEDGD-----RLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALL----------RADP--------ELI 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 357 DMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKG--VVVMIPSyvLHHDPKYWTEPEKFLPERfskKNKDNIdpyiytP 434
Cdd:cd20625  246 PAAVEELLRYDSPVQLTARVALEDVEIGGQTIPAGdrVLLLLGA--ANRDPAVFPDPDRFDITR---APNRHL------A 314
                        330       340
                 ....*....|....*....|....*....
gi 608788355 435 FGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20625  315 FGAGIHFCLGAPLARLEAEIALRALLRRF 343
PLN02774 PLN02774
brassinosteroid-6-oxidase
249-450 1.21e-15

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 79.43  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 249 LTKSVKQIKEGRLKETQKHRvDFL-QLMidsqnsKDSETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDV 327
Cdd:PLN02774 225 IVRMLRQLIQERRASGETHT-DMLgYLM------RKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKA 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 328 QQKVQKEIDTVLPNKAPP---TYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHD 404
Cdd:PLN02774 298 LQELRKEHLAIRERKRPEdpiDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMELNGYVIPKGWRIYVYTREINYD 377
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 608788355 405 PKYWTEPEKFLPERFSKKNKDNiDPYIYTpFGSGPRNCIGMRFALV 450
Cdd:PLN02774 378 PFLYPDPMTFNPWRWLDKSLES-HNYFFL-FGGGTRLCPGKELGIV 421
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
298-466 7.92e-15

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 76.97  E-value: 7.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 298 QSIIF--IFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNkapptyDTVLQLEYLDMVVNETLRLFP-VAMRLE 374
Cdd:PLN02169 303 RDVIFslVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN------EDLEKLVYLHAALSESMRLYPpLPFNHK 376
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 375 RVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTE-PEKFLPERFSKKNKD--NIDPYIYTPFGSGPRNCIGMRFALVN 451
Cdd:PLN02169 377 APAKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEdALDFKPERWISDNGGlrHEPSYKFMAFNSGPRTCLGKHLALLQ 456
                        170
                 ....*....|....*
gi 608788355 452 MKLALVRVLQNFSFK 466
Cdd:PLN02169 457 MKIVALEIIKNYDFK 471
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
268-460 3.90e-14

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: 73.94  E-value: 3.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 268 RVDFLQLMIDSQNSKDSethkaLSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKeiDTVLPNKAppty 347
Cdd:cd11038  193 GDDLISTLVAAEQDGDR-----LSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHPDQWRALRE--DPELAPAA---- 261
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 348 dtvlqleyldmvVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKywtepeKFLPERF--SKKNKD 425
Cdd:cd11038  262 ------------VEEVLRWCPTTTWATREAVEDVEYNGVTIPAGTVVHLCSHAANRDPR------VFDADRFdiTAKRAP 323
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 608788355 426 NIDpyiytpFGSGPRNCIGMRFALVNMKLALvRVL 460
Cdd:cd11038  324 HLG------FGGGVHHCLGAFLARAELAEAL-TVL 351
PLN02500 PLN02500
cytochrome P450 90B1
287-466 9.67e-14

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 73.36  E-value: 9.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 287 HKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLPNK-----APPTYDTVLQLEYLDMVVN 361
Cdd:PLN02500 272 HSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEHLEIARAKkqsgeSELNWEDYKKMEFTQCVIN 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 362 ETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKN-------KDNIDPYIYTP 434
Cdd:PLN02500 352 ETLRLGNVVRFLHRKALKDVRYKGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNnrggssgSSSATTNNFMP 431
                        170       180       190
                 ....*....|....*....|....*....|..
gi 608788355 435 FGSGPRNCIGMRFALVNMKLALVRVLQNFSFK 466
Cdd:PLN02500 432 FGGGPRLCAGSELAKLEMAVFIHHLVLNFNWE 463
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
285-463 1.12e-13

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: 73.10  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 285 ETHKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLP---NKAPPTYDTVL------QLEY 355
Cdd:cd20632  206 EQYDVLQDYDKAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEIDHVLQstgQELGPDFDIHLtreqldSLVY 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 356 LDMVVNETLRLFPVAMRLeRVCKKD----VEINGMF-IPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNID-- 428
Cdd:cd20632  286 LESAINESLRLSSASMNI-RVVQEDftlkLESDGSVnLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRFVEDGKKKTTfy 364
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 608788355 429 ------PYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20632  365 krgqklKYYLMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYF 405
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
249-448 3.09e-13

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 71.69  E-value: 3.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 249 LTKSVKQIKEGRLKETQKHRVDFLQL---MIDS--QNSKDSETHKALSD--LELMaqsiifiFAGYETTSSVLSFIIYEL 321
Cdd:PLN03141 206 MVKLVKKIIEEKRRAMKNKEEDETGIpkdVVDVllRDGSDELTDDLISDnmIDMM-------IPGEDSVPVLMTLAVKFL 278
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 322 ATHPDVQQKVQKEIDTVLPNKA----PPTYDTVLQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIP 397
Cdd:PLN03141 279 SDCPVALQQLTEENMKLKRLKAdtgePLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEIKGYLIPKGWCVLAY 358
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 608788355 398 SYVLHHDPKYWTEPEKFLPERFSKKNKDNIDpyiYTPFGSGPRNCIGMRFA 448
Cdd:PLN03141 359 FRSVHLDEENYDNPYQFNPWRWQEKDMNNSS---FTPFGGGQRLCPGLDLA 406
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
300-463 4.78e-13

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 71.14  E-value: 4.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 300 IIF--IFAGYETTSSVLSFIIYELATH-PDVQQKVQKEIDTVLPNKAPPTYDTVLQLEYLDMVVNETLRLFP-VAMRLER 375
Cdd:cd11071  229 LLFmlGFNAFGGFSALLPSLLARLGLAgEELHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPpVPLQYGR 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 376 VcKKDVEIN---GMF-IPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDpYIYtpFGSGP---------RNC 442
Cdd:cd11071  309 A-RKDFVIEshdASYkIKKGELLVGYQPLATRDPKVFDNPDEFVPDRFMGEEGKLLK-HLI--WSNGPeteeptpdnKQC 384
                        170       180
                 ....*....|....*....|.
gi 608788355 443 IGMRFALVNMKLALVRVLQNF 463
Cdd:cd11071  385 PGKDLVVLLARLFVAELFLRY 405
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
290-460 8.06e-13

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: 69.86  E-value: 8.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 290 LSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKeiDTVLPNKApptydtvlqleyldmvVNETLRLF-P 368
Cdd:cd11033  205 LTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRA--DPSLLPTA----------------VEEILRWAsP 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 369 VA-MRleRVCKKDVEINGMFIPKG--VVVMIPSyvLHHDPKYWTEPEKFLPERfskknkdnidpyiyTP-----FGSGPR 440
Cdd:cd11033  267 VIhFR--RTATRDTELGGQRIRAGdkVVLWYAS--ANRDEEVFDDPDRFDITR--------------SPnphlaFGGGPH 328
                        170       180
                 ....*....|....*....|
gi 608788355 441 NCIGMRFALVNMKLALVRVL 460
Cdd:cd11033  329 FCLGAHLARLELRVLFEELL 348
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
302-460 1.02e-12

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 69.53  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 302 FIFAGYETTSSVLSFIIYELATHPDVQQKVQKEidtvlPNKAPPtydtvlqleyldmVVNETLRLFPVAMRLERVCKKDV 381
Cdd:cd11037  210 YLSAGLDTTISAIGNALWLLARHPDQWERLRAD-----PSLAPN-------------AFEEAVRLESPVQTFSRTTTRDT 271
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 382 EINGMFIPKG--VVVMIPSyvLHHDPKYWTEPEKFLPERfskknkdniDPYIYTPFGSGPRNCIGMRFALVNMKlALVRV 459
Cdd:cd11037  272 ELAGVTIPAGsrVLVFLGS--ANRDPRKWDDPDRFDITR---------NPSGHVGFGHGVHACVGQHLARLEGE-ALLTA 339

                 .
gi 608788355 460 L 460
Cdd:cd11037  340 L 340
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
289-460 2.32e-12

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 68.65  E-value: 2.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 289 ALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKeiDTVLPNKApptydtvlqleyldmvVNETLRLFP 368
Cdd:cd11080  188 ALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA--DRSLVPRA----------------IAETLRYHP 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 369 VAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPER--------FSKKNKdnidpyiYTPFGSGPR 440
Cdd:cd11080  250 PVQLIPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPDTFNIHRedlgirsaFSGAAD-------HLAFGSGRH 322
                        170       180
                 ....*....|....*....|
gi 608788355 441 NCIGMRFALVNMKLALVRVL 460
Cdd:cd11080  323 FCVGAALAKREIEIVANQVL 342
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
314-456 4.07e-12

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 67.94  E-value: 4.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 314 LSFIIYELATHPDVQQKVQKEIDtvlpnkapptydtvlqlEYLDMVVNETLRL---FPVAMrlERVcKKDVEINGMFIPK 390
Cdd:cd11067  240 VTFAALALHEHPEWRERLRSGDE-----------------DYAEAFVQEVRRFypfFPFVG--ARA-RRDFEWQGYRFPK 299
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 608788355 391 GVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKnkdNIDPYIYTPFGSGP-----RnCIGMRFALVNMKLAL 456
Cdd:cd11067  300 GQRVLLDLYGTNHDPRLWEDPDRFRPERFLGW---EGDPFDFIPQGGGDhatghR-CPGEWITIALMKEAL 366
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
128-463 4.34e-12

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: 67.94  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 128 RIRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLrreaETGKPVTLKHVFgAY--SMDVItSTSFGVSIDSlnnpQDPFVE 205
Cdd:cd11029   83 RLRRLVAKAFTPRRVEALRPRIEEITDELLDAL----AARGVVDLVADF-AYplPITVI-CELLGVPEED----RDRFRR 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 206 NTKKLLRFNPlDPfvlsikvfpflTPILEALnitvfpRKVISFLTKSVKQiKEGRLKEtqkhrvDFLQLMIDSQNSKDse 285
Cdd:cd11029  153 WSDALVDTDP-PP-----------EEAAAAL------RELVDYLAELVAR-KRAEPGD------DLLSALVAARDEGD-- 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 286 thkALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVqkeidtvlpnKAPPtydtvlqlEYLDMVVNETLR 365
Cdd:cd11029  206 ---RLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALL----------RADP--------ELWPAAVEELLR 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 366 LF-PVAMRLERVCKKDVEINGMFIPKGVVVMIpSYV-LHHDPKYWTEPEKFLPERfskKNKDNIdpyiytPFGSGPRNCI 443
Cdd:cd11029  265 YDgPVALATLRFATEDVEVGGVTIPAGEPVLV-SLAaANRDPARFPDPDRLDITR---DANGHL------AFGHGIHYCL 334
                        330       340
                 ....*....|....*....|
gi 608788355 444 GMRFALVNMKLALVRVLQNF 463
Cdd:cd11029  335 GAPLARLEAEIALGALLTRF 354
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
241-465 3.89e-11

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: 65.08  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 241 FPRKVISFLTKSVKqikegrlKETQKHRVDFLQLMIDSQNSKD-------SETHKALSDL---ELMAQSIIFIF--AGYE 308
Cdd:cd20633  166 FPRLAYSVLPPKDK-------LEAERLKRLFWDMLSVSKMSQKenisgwiSEQQRQLAEHgmpEYMQDRFMFLLlwASQG 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 309 TTSSVLSFIIYELATHPDVQQKVQKEIDTVL--------PNKAPP--TYDTVLQLEYLDMVVNETLRLfPVAMRLERVCK 378
Cdd:cd20633  239 NTGPASFWLLLYLLKHPEAMKAVREEVEQVLketgqevkPGGPLInlTRDMLLKTPVLDSAVEETLRL-TAAPVLIRAVV 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 379 KDVEI---NG--MFIPKG-VVVMIPSYVLHHDPKYWTEPEKFLPERFSK----------KNKDNIDPYIyTPFGSGPRNC 442
Cdd:cd20633  318 QDMTLkmaNGreYALRKGdRLALFPYLAVQMDPEIHPEPHTFKYDRFLNpdggkkkdfyKNGKKLKYYN-MPWGAGVSIC 396
                        250       260
                 ....*....|....*....|...
gi 608788355 443 IGMRFALVNMKLALVRVLQNFSF 465
Cdd:cd20633  397 PGRFFAVNEMKQFVFLMLTYFDL 419
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
270-463 3.91e-11

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 64.85  E-value: 3.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 270 DFLQLMIDSQNSKDsethkALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDvqqkvQKEidtVLpnKAPPtydt 349
Cdd:cd11030  189 DLLSRLVAEHGAPG-----ELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPE-----QLA---AL--RADP---- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 350 vlqlEYLDMVVNETLRLFPVA-MRLERVCKKDVEINGMFIPKG--VVVMIPSyvLHHDPKYWTEPEKFLPERfskKNKDN 426
Cdd:cd11030  250 ----SLVPGAVEELLRYLSIVqDGLPRVATEDVEIGGVTIRAGegVIVSLPA--ANRDPAVFPDPDRLDITR---PARRH 320
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 608788355 427 IdpyiytPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd11030  321 L------AFGHGVHQCLGQNLARLELEIALPTLFRRF 351
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
356-460 4.87e-10

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 61.20  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 356 LDMVVNETLRLFPVAMRLERVCKKDVEINGMF-----IPKGVVVMIPSYVLHHDPKYWTEPEKFLPERfskknkdNIDPY 430
Cdd:cd20612  240 LRGYVLEALRLNPIAPGLYRRATTDTTVADGGgrtvsIKAGDRVFVSLASAMRDPRAFPDPERFRLDR-------PLESY 312
                         90       100       110
                 ....*....|....*....|....*....|
gi 608788355 431 IYtpFGSGPRNCIGMRFALVNMKlALVRVL 460
Cdd:cd20612  313 IH--FGHGPHQCLGEEIARAALT-EMLRVV 339
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
321-471 1.45e-09

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: 59.78  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 321 LATHPDVQQKVQKEIDTvlPNKAPPtydtvlqLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYV 400
Cdd:cd20624  218 LAAHPEQAARAREEAAV--PPGPLA-------RPYLRACVLDAVRLWPTTPAVLRESTEDTVWGGRTVPAGTGFLIFAPF 288
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 608788355 401 LHHDPKYWTEPEKFLPERFSKKNKDNIDPYIytPFGSGPRNCIGMRFALVNMKLALVRVLQNFSFKPCKET 471
Cdd:cd20624  289 FHRDDEALPFADRFVPEIWLDGRAQPDEGLV--PFSAGPARCPGENLVLLVASTALAALLRRAEIDPLESP 357
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
207-463 8.30e-09

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 57.77  E-value: 8.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 207 TKKLLRFNPLDPFVLSIKVFPFLtpiLEALNITVFPRKvisflTKSVKQIKEGRLKETQKHRVDFLQLMidSQNSKDSET 286
Cdd:cd20631  150 AQRALILNALENFKEFDKVFPAL---VAGLPIHMFKTA-----KSAREALAERLLHENLQKRENISELI--SLRMLLNDT 219
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 287 HKALSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTVLpNKAPPTYD--------TVLQLE---Y 355
Cdd:cd20631  220 LSTLDEMEKARTHVAMLWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTL-EKTGQKVSdggnpivlTREQLDdmpV 298
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 356 LDMVVNETLRLFPVAMRLeRVCKKDVEI---NGMF--IPKG-VVVMIPSyVLHHDPKYWTEPEKFLPERFSKKN-KDNID 428
Cdd:cd20631  299 LGSIIKEALRLSSASLNI-RVAKEDFTLhldSGESyaIRKDdIIALYPQ-LLHLDPEIYEDPLTFKYDRYLDENgKEKTT 376
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 608788355 429 --------PYIYTPFGSGPRNCIGMRFALVNMKLALVRVLQNF 463
Cdd:cd20631  377 fykngrklKYYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYF 419
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
321-489 1.14e-07

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 54.38  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 321 LATHPDVQQKVQKEIDTVLPNKAPP--TYDTVLQLEY-----LDMVVNETLRLfPVAMRLERVCKKDVEI---NG--MFI 388
Cdd:cd20634  248 LLKHPEAMAAVRGEIQRIKHQRGQPvsQTLTINQELLdntpvFDSVLSETLRL-TAAPFITREVLQDMKLrlaDGqeYNL 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 389 PKG-VVVMIPSYVLHHDPKYWTEPEKFLPERF------SKKN--KDNIDPYIYT-PFGSGPRNCIGMRFALVNMKLALVR 458
Cdd:cd20634  327 RRGdRLCLFPFLSPQMDPEIHQEPEVFKYDRFlnadgtEKKDfyKNGKRLKYYNmPWGAGDNVCIGRHFAVNSIKQFVFL 406
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 608788355 459 VLQNFSFKPC-KETQIPL--KLRFG-GLLLTEKPI 489
Cdd:cd20634  407 ILTHFDVELKdPEAEIPEfdPSRYGfGLLQPEGDI 441
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
290-461 1.43e-05

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 47.35  E-value: 1.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 290 LSDLELMaqSIIFIFAGYETTSSVLSF--IIYELATHPDVQQKVQKeidtvlpnkapptydtvlQLEYLDMVVNETLRLF 367
Cdd:cd11079  179 LTDEEIV--SILRNWTVGELGTIAACVgvLVHYLARHPELQARLRA------------------NPALLPAAIDEILRLD 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 368 -P-VAMRleRVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERfskknkDNIDPYIYtpfGSGPRNCIGM 445
Cdd:cd11079  239 dPfVANR--RITTRDVELGGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR------HAADNLVY---GRGIHVCPGA 307
                        170
                 ....*....|....*.
gi 608788355 446 RFALVNMKLALVRVLQ 461
Cdd:cd11079  308 PLARLELRILLEELLA 323
CYP_XplA cd20619
cytochrome P450 XplA; XplA is a cytochrome P450 that was found to mediate the microbial ...
342-444 7.08e-05

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


Pssm-ID: 410712 [Multi-domain]  Cd Length: 358  Bit Score: 45.11  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 342 KAPPTYDTV-LQLEYLDMVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFS 420
Cdd:cd20619  219 RRPEVFTAFrNDESARAAIINEMVRMDPPQLSFLRFPTEDVEIGGVLIEAGSPIRFMIGAANRDPEVFDDPDVFDHTRPP 298
                         90       100
                 ....*....|....*....|....
gi 608788355 421 KKNKDnidpyiyTPFGSGPRNCIG 444
Cdd:cd20619  299 AASRN-------LSFGLGPHSCAG 315
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
290-448 2.58e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 43.26  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 290 LSDLELMAQSIIFIFAGYETTSSVLSFIIYELATHPDVQQKVQKEIDTvlpnkAPPTYDtvlqlEYLDMVVnetlrlfPV 369
Cdd:cd11039  198 MSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVMAGDVH-----WLRAFE-----EGLRWIS-------PI 260
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 370 AMRlERVCKKDVEINGMFIPKGVVVMIPSYVLHHDPKYWTEPEKFlpERFSKKNKdnidpyiYTPFGSGPRNCIGMRFA 448
Cdd:cd11039  261 GMS-PRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRF--DVFRPKSP-------HVSFGAGPHFCAGAWAS 329
PLN02648 PLN02648
allene oxide synthase
301-432 5.56e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 42.61  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 301 IFIFAGYETTSSVLSFIIYELATH-PDVQQKVQKEIDTVLPNKAP-PTYDTVLQLEYLDMVVNETLRLFP-VAMRLERVc 377
Cdd:PLN02648 279 VLGFNAFGGFKIFFPALLKWVGRAgEELQARLAEEVRSAVKAGGGgVTFAALEKMPLVKSVVYEALRIEPpVPFQYGRA- 357
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 608788355 378 KKDVEIN---GMF-IPKGVVVMIPSYVLHHDPKYWTEPEKFLPERFSKKNKDNIDPYIY 432
Cdd:PLN02648 358 REDFVIEshdAAFeIKKGEMLFGYQPLVTRDPKVFDRPEEFVPDRFMGEEGEKLLKYVF 416
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
354-448 6.53e-04

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 42.09  E-value: 6.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 354 EYLDMVVNETLRLFPVAmRLE-RVCKKDVEINGMFIPKG--VVVMIPSyvLHHDPKYWTEPEKFLPERfskknkdniDPY 430
Cdd:cd11036  219 ELAAAAVAETLRYDPPV-RLErRFAAEDLELAGVTLPAGdhVVVLLAA--ANRDPEAFPDPDRFDLGR---------PTA 286
                         90
                 ....*....|....*...
gi 608788355 431 IYTPFGSGPRNCIGMRFA 448
Cdd:cd11036  287 RSAHFGLGRHACLGAALA 304
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
358-444 1.88e-03

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. 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: 410719  Cd Length: 381  Bit Score: 40.85  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 608788355 358 MVVNETLRLFPVAMRLERVCKKDVEINGMFIPKGVVVMipsyvlHHDPKYW-TEPEKFLPERFSKKNKDNIDPYIytPFG 436
Cdd:cd20626  260 NLVKEALRLYPPTRRIYRAFQRPGSSKPEIIAADIEAC------HRSESIWgPDALEFNPSRWSKLTPTQKEAFL--PFG 331

                 ....*...
gi 608788355 437 SGPRNCIG 444
Cdd:cd20626  332 SGPFRCPA 339
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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