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Conserved domains on  [gi|117292|sp|P19098|]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
71-484 0e+00

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  Cd Length: 414  Bit Score: 848.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    71 NACNYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKA 150
Cdd:cd20616   1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   151 LSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQNYFDAWQALLLKP 230
Cdd:cd20616  81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   231 DIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTL 310
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   311 SVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKG 390
Cdd:cd20616 241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   391 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNI 470
Cdd:cd20616 321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                       410
                ....*....|....
gi 117292   471 QKNNDLSMHPIERQ 484
Cdd:cd20616 401 QKTNDLSLHPDETQ 414
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
71-484 0e+00

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  Cd Length: 414  Bit Score: 848.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    71 NACNYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKA 150
Cdd:cd20616   1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   151 LSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQNYFDAWQALLLKP 230
Cdd:cd20616  81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   231 DIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTL 310
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   311 SVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKG 390
Cdd:cd20616 241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   391 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNI 470
Cdd:cd20616 321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                       410
                ....*....|....
gi 117292   471 QKNNDLSMHPIERQ 484
Cdd:cd20616 401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-487 1.67e-122

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: 366.60  E-value: 1.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292      47 PGPGYCMGIGPLISHgrflWMGVGNACNYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNY--VSRFGSKLGLQCI 124
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     125 GMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLG 204
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     205 VPLD------ESAIVLKIQNYFD-----AWQALLLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKldE 273
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     274 HMDFASQLIFAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGD-REVQSDDM 349
Cdd:pfam00067 238 PRDFLDALLLAKEEEDgskLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     350 PNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPS 423
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117292     424 RYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNDLSMHPIERQPLL 487
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
93-458 2.04e-35

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 136.79  E-value: 2.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    93 TFIISKSSSVFHVMKHWNYVSRFGSKLGLQCIG--MYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTIVH 170
Cdd:COG2124  50 FWVVSRPADVREVLRDPRFFSSALGAGLRPRLLrpVLGDGSLLTLDGPEHTRLRKLLAPAFTPRALRGYRPLIREIADRL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   171 LDKLEEVTTEVgnvnVLNLMRRIMLDTSNKLFlGVPLDESAIvlkiqnyFDAWQALLLkpDIFFKISWLCKKYEEAAKDL 250
Cdd:COG2124 130 LDDLWQGGADL----VLDFAAELTLRVIAELL-GVPLEDRPQ-------LLRWSDALL--LRLDPDLGPEEPWRRARAAR 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   251 KGAMEI---LIEQKRqklstvekLDEHMDFASQLIFAQNRGDLT---AENVNQCVLeMMIAAPDTLSVTLFIMLILIADD 324
Cdd:COG2124 196 RELDAYlraLIAERR--------AAPRDDLLSLLLSAEDDGGGRlsdDEIRDELIT-LLVAGHETTANALAWALYALLRH 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   325 PTVEEKMMREietvmgdrevqsddmPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE 404
Cdd:COG2124 267 PDQLAKLRAE---------------PDRPLLEAVVEETLRLYPPVPLARRVATEDVELGGYRIPAGTVVLLSIGAANRDP 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 117292   405 -FFPKPNEFSLENFEKNvpsryFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCR 458
Cdd:COG2124 332 eVFPDPDEFDPERFNNA-----HLPFGGGPHRCLGAALARLELKVALAELLRRFP 381
PLN02738 PLN02738
carotene beta-ring hydroxylase
140-464 4.59e-21

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 96.52  E-value: 4.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    140 WKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLD----ESAIVLK 215
Cdd:PLN02738 222 WRVRRRAIVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDslsnDTGIVEA 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    216 IQNY-----------FDAWQALLLKpdiffKISWLCKKYEEAAKDLKGAMEILIEQ-KRqkLSTVEKL---DEHMDF--A 278
Cdd:PLN02738 302 VYTVlreaedrsvspIPVWEIPIWK-----DISPRQRKVAEALKLINDTLDDLIAIcKR--MVEEEELqfhEEYMNErdP 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    279 SQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVEN 357
Cdd:PLN02738 375 SILHFLLASGDdVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTR 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    358 FIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-------LEFF---------PKPNEfSLENFeknv 421
Cdd:PLN02738 455 VINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNF---- 529
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 117292    422 psRYFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKG 464
Cdd:PLN02738 530 --SYL-PFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPG 569
CYP450_TxtE TIGR04458
4-nitrotryptophan synthase; Members of this family are cytochrome P450 enzymes that convert ...
268-456 2.75e-06

4-nitrotryptophan synthase; Members of this family are cytochrome P450 enzymes that convert L-tryptophan into L-4-nitrotryptophan. In thaxtomin gene clusters, this enzyme (TxtE) uses nitric acid (NO) derived from arginine by the nitric oxide synthase TxtD, and O2, to perform the tryptophan nitration. L-4-nitrotryptophan is then used as a non-proteinogenic amino acid by non-ribosomal peptide synthases (NRPS).


Pssm-ID: 275251  Cd Length: 403  Bit Score: 49.48  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     268 VEKLDEHMDFASQLIFAQnRGDLTAENVnqcvLEMMIAAPDTLSVT-----------LFIMLILIADDPTVEEKMM---- 332
Cdd:TIGR04458 187 LELLTDLHTYASELLEGK-RGKVLPDTV----IARLAAAQDGLTETtpeqtvhqlvlLFIALFAPTTPGSLSSGMLafar 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     333 --REIETVMGDREVqsddmpnlkiVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKP 409
Cdd:TIGR04458 262 npDQIERFLADPAC----------VDNTANEVVRYNASNQFTWRVATTDVDMGGVRIKAGQAVALFLGAANRdPEVFERP 331
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 117292     410 NEFSLENFEknvpSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:TIGR04458 332 NDFDLDRPN----SGRHLSFGQGVHACLGRQIASLQLKWFFVALLGR 374
 
Name Accession Description Interval E-value
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
71-484 0e+00

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  Cd Length: 414  Bit Score: 848.95  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    71 NACNYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNYVSRFGSKLGLQCIGMYENGIIFNNNPAHWKEIRPFFTKA 150
Cdd:cd20616   1 SACNYYNKMYGEFVRVWISGEETLIISKSSAVFHVLKHSHYTSRFGSKLGLQCIGMHENGIIFNNNPALWKKVRPFFAKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   151 LSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQNYFDAWQALLLKP 230
Cdd:cd20616  81 LTGPGLVRMVTVCVESTNTHLDNLEEVTNESGYVDVLTLMRRIMLDTSNRLFLGVPLNEKAIVLKIQGYFDAWQALLIKP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   231 DIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTL 310
Cdd:cd20616 161 DIFFKISWLYKKYEKAVKDLKDAIEILIEQKRRRISTAEKLEDHMDFATELIFAQKRGELTAENVNQCVLEMLIAAPDTM 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   311 SVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKG 390
Cdd:cd20616 241 SVSLFFMLLLIAQHPEVEEAILKEIQTVLGERDIQNDDLQKLKVLENFINESMRYQPVVDFVMRKALEDDVIDGYPVKKG 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   391 TNIILNIGRMHKLEFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNI 470
Cdd:cd20616 321 TNIILNIGRMHRLEFFPKPNEFTLENFEKNVPSRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRCVENI 400
                       410
                ....*....|....
gi 117292   471 QKNNDLSMHPIERQ 484
Cdd:cd20616 401 QKTNDLSLHPDETQ 414
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
47-487 1.67e-122

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: 366.60  E-value: 1.67e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292      47 PGPGYCMGIGPLISHgrflWMGVGNACNYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNY--VSRFGSKLGLQCI 124
Cdd:pfam00067   4 PPPLPLFGNLLQLGR----KGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEefSGRPDEPWFATSR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     125 GMYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLG 204
Cdd:pfam00067  80 GPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     205 VPLD------ESAIVLKIQNYFD-----AWQALLLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKldE 273
Cdd:pfam00067 160 ERFGsledpkFLELVKAVQELSSllsspSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAKK--S 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     274 HMDFASQLIFAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGD-REVQSDDM 349
Cdd:pfam00067 238 PRDFLDALLLAKEEEDgskLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDkRSPTYDDL 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     350 PNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF----EKNVPS 423
Cdd:pfam00067 318 QNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRdPEVFPNPEEFDPERFldenGKFRKS 397
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117292     424 RYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNDLSMHPIERQPLL 487
Cdd:pfam00067 398 FAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIDETPGLLLPPKPYKLKF 461
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
81-460 1.13e-60

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: 204.29  E-value: 1.13e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    81 GEFVRVWISGEETFIISKSSSVFHVMKHWNYVSRFGSKLGLQCIGMYENGIiFNNNPAHWKEIRPFFTKALSGPGLVRMI 160
Cdd:cd00302   1 GPVFRVRLGGGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGL-LTLDGPEHRRLRRLLAPAFTPRALAALR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   161 AICVESTIVHLDKLEEVTTevGNVNVLNLMRRIMLDTSNKLFLGVPLDESAivLKIQNYFDAWQALLLKPDIFFKISWLC 240
Cdd:cd00302  80 PVIREIARELLDRLAAGGE--VGDDVADLAQPLALDVIARLLGGPDLGEDL--EELAELLEALLKLLGPRLLRPLPSPRL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   241 KKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDfasqlifAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLIL 320
Cdd:cd00302 156 RRLRRARARLRDYLEELIARRRAEPADDLDLLLLAD-------ADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   321 IADDPTVEEKMMREIETVMGDREVqsDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRM 400
Cdd:cd00302 229 LARHPEVQERLRAEIDAVLGDGTP--EDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVELGGYTIPAGTLVLLSLYAA 306
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117292   401 HKLE-FFPKPNEFSLENF--EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQ 460
Cdd:cd00302 307 HRDPeVFPDPDEFDPERFlpEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFE 369
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
81-482 2.26e-45

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: 163.92  E-value: 2.26e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    81 GEFVRVWISGEETFIISKSSSV--FHVMKHWNYVSRFGSKLGLqcIGMYENGIIFNNNPaHWKEIRPFFTKALSGPGLVR 158
Cdd:cd20617   1 GGIFTLWLGDVPTVVLSDPEIIkeAFVKNGDNFSDRPLLPSFE--IISGGKGILFSNGD-YWKELRRFALSSLTKTKLKK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   159 ----MIAICVESTIVHLDKLEEVTTE----------VGNVnVLNLM--RRIMLDTSNK-LFLGVPLDESAIVLKIQNYFD 221
Cdd:cd20617  78 kmeeLIEEEVNKLIESLKKHSKSGEPfdprpyfkkfVLNI-INQFLfgKRFPDEDDGEfLKLVKPIEEIFKELGSGNPSD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   222 awqaLLLKPDIFFKISWlcKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLE 301
Cdd:cd20617 157 ----FIPILLPFYFLYL--KKLKKSYDKIKDFIEKIIEEHLKTIDPNNPRDLIDDELLLLLKEGDSGLFDDDSIISTCLD 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   302 MMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG-DREVQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQD 379
Cdd:cd20617 231 LFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGnDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLpRVTTED 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   380 DVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENF---EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20617 311 TEIGGYFIPKGTQIIINIYSLHRDEkYFEDPEEFNPERFlenDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLLL 390
                       410       420
                ....*....|....*....|....*..
gi 117292   456 RCRVQTMKGRgLNNIQKNNDLSMHPIE 482
Cdd:cd20617 391 NFKFKSSDGL-PIDEKEVFGLTLKPKP 416
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
81-487 8.07e-43

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: 156.97  E-value: 8.07e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    81 GEFVRVWISGEETFIISKSSSVFHVM--KHWNYVS-----RFGSKLGlqcigmyeNGIIfNNNPAHWKEIR----PFFT- 148
Cdd:cd20620   1 GDVVRLRLGPRRVYLVTHPDHIQHVLvtNARNYVKggvyeRLKLLLG--------NGLL-TSEGDLWRRQRrlaqPAFHr 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   149 KALSGpglvrMIAICVESTIVHLDKLEEVTTEvGNVNVLNLMRRIMLDTSNKLFLGVPLDE-------------SAIVLK 215
Cdd:cd20620  72 RRIAA-----YADAMVEATAALLDRWEAGARR-GPVDVHAEMMRLTLRIVAKTLFGTDVEGeadeigdaldvalEYAARR 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   216 IQNYFDAWQALLLKPDiffkiswlcKKYEEAAKDLKGAMEILIEQKRQklstvEKLDEHmDFASQLIFAQNRGDLTAENV 295
Cdd:cd20620 146 MLSPFLLPLWLPTPAN---------RRFRRARRRLDEVIYRLIAERRA-----APADGG-DLLSMLLAARDEETGEPMSD 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   296 NQC---VLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLI 372
Cdd:cd20620 211 QQLrdeVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLGGRPPTAEDLPQLPYTEMVLQESLRLYPPAWII 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   373 MRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSR-----YFqPFGFGPRGCVGKFIAMVMM 446
Cdd:cd20620 291 GREAVEDDEIGGYRIPAGSTVLISPYVTHRDPrFWPDPEAFDPERFTPEREAArpryaYF-PFGGGPRICIGNHFAMMEA 369
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 117292   447 KAILVTLLRRCRVQTMKGrglnniqknndlsmHPIERQPLL 487
Cdd:cd20620 370 VLLLATIAQRFRLRLVPG--------------QPVEPEPLI 396
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
81-466 6.52e-39

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: 146.51  E-value: 6.52e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    81 GEFVRVWISGEETFIISKS-------SSVFHVMKHWNYvSRFGSKLGlqcigmyeNGIIFNNNPaHWKEIRPFFTKALSG 153
Cdd:cd20628   1 GGVFRLWIGPKPYVVVTNPedievilSSSKLITKSFLY-DFLKPWLG--------DGLLTSTGE-KWRKRRKLLTPAFHF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   154 PGLVRMIAICVESTIVHLDKLEEVTtEVGNVNVLNLMRR----IMLDTSnklfLGVPLDE-----SAIVLKIQNYFDAWQ 224
Cdd:cd20628  71 KILESFVEVFNENSKILVEKLKKKA-GGGEFDIFPYISLctldIICETA----MGVKLNAqsnedSEYVKAVKRILEIIL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   225 A----LLLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQ----------LIFAQNRGDL 290
Cdd:cd20628 146 KrifsPWLRFDFIFRLTSLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDDEFGKkkrkafldllLEAHEDGGPL 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   291 TAENVNQCVLEMMIAAPDTLSVTL-FImLILIADDPTVEEKMMREIETVMGD--REVQSDDMPNLKIVENFIYESMRYQP 367
Cdd:cd20628 226 TDEDIREEVDTFMFAGHDTTASAIsFT-LYLLGLHPEVQEKVYEELDEIFGDddRRPTLEDLNKMKYLERVIKETLRLYP 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   368 VVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENFEK-NVPSRY---FQPFGFGPRGCVG-KFi 441
Cdd:cd20628 305 SVPFIGRRLTEDIKLDGYTIPKGTTVVISIYALHRNpEYFPDPEKFDPDRFLPeNSAKRHpyaYIPFSAGPRNCIGqKF- 383
                       410       420
                ....*....|....*....|....*
gi 117292   442 AMVMMKAILVTLLRRCRVQTMKGRG 466
Cdd:cd20628 384 AMLEMKTLLAKILRNFRVLPVPPGE 408
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
130-461 8.46e-38

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: 143.44  E-value: 8.46e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   130 GIIFNNNPaHWKEIRPFFTKALSGPGLVRMiaicvestivHLDKLEEVTTE-------------VGNVNVLNLMRR---- 192
Cdd:cd11054  57 GLLNSNGE-EWHRLRSAVQKPLLRPKSVAS----------YLPAINEVADDfverirrlrdedgEEVPDLEDELYKwsle 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   193 ----IMLDTSNKLFLGVPLDESAIVLK-IQNYFDAWQALLLKPDIFFKI---SWlcKKYEEAAKDLKGAMEILIEQKRQK 264
Cdd:cd11054 126 sigtVLFGKRLGCLDDNPDSDAQKLIEaVKDIFESSAKLMFGPPLWKYFptpAW--KKFVKAWDTIFDIASKYVDEALEE 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   265 LSTVEKLDEH-MDFASQLIfaqNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDRE 343
Cdd:cd11054 204 LKKKDEEDEEeDSLLEYLL---SKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGE 280
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   344 -VQSDDMPNLKIVENFIYESMRYQPVVDLIMRKaLQDD-VIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLE----- 415
Cdd:cd11054 281 pITAEDLKKMPYLKACIKESLRLYPVAPGNGRI-LPKDiVLSGYHIPKGTLVVLSNYVMGRDEeYFPDPEEFIPErwlrd 359
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 117292   416 NFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQT 461
Cdd:cd11054 360 DSENKNIHPFaSLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEY 406
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
93-458 2.04e-35

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 136.79  E-value: 2.04e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    93 TFIISKSSSVFHVMKHWNYVSRFGSKLGLQCIG--MYENGIIFNNNPAHWKEIRPFFTKALSGPGLVRMIAICVESTIVH 170
Cdd:COG2124  50 FWVVSRPADVREVLRDPRFFSSALGAGLRPRLLrpVLGDGSLLTLDGPEHTRLRKLLAPAFTPRALRGYRPLIREIADRL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   171 LDKLEEVTTEVgnvnVLNLMRRIMLDTSNKLFlGVPLDESAIvlkiqnyFDAWQALLLkpDIFFKISWLCKKYEEAAKDL 250
Cdd:COG2124 130 LDDLWQGGADL----VLDFAAELTLRVIAELL-GVPLEDRPQ-------LLRWSDALL--LRLDPDLGPEEPWRRARAAR 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   251 KGAMEI---LIEQKRqklstvekLDEHMDFASQLIFAQNRGDLT---AENVNQCVLeMMIAAPDTLSVTLFIMLILIADD 324
Cdd:COG2124 196 RELDAYlraLIAERR--------AAPRDDLLSLLLSAEDDGGGRlsdDEIRDELIT-LLVAGHETTANALAWALYALLRH 266
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   325 PTVEEKMMREietvmgdrevqsddmPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE 404
Cdd:COG2124 267 PDQLAKLRAE---------------PDRPLLEAVVEETLRLYPPVPLARRVATEDVELGGYRIPAGTVVLLSIGAANRDP 331
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*
gi 117292   405 -FFPKPNEFSLENFEKNvpsryFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCR 458
Cdd:COG2124 332 eVFPDPDEFDPERFNNA-----HLPFGGGPHRCLGAALARLELKVALAELLRRFP 381
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
82-464 2.40e-33

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: 131.17  E-value: 2.40e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    82 EFVRVWISGEETFIISKSSSVFHVMKH--WNYV------SRFGSKLGlqcigmyeNGIiFNNNPAHWKEIRPFFTKALSG 153
Cdd:cd11064   2 TFRGPWPGGPDGIVTADPANVEHILKTnfDNYPkgpefrDLFFDLLG--------DGI-FNVDGELWKFQRKTASHEFSS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   154 PGLVRMIAICV-ESTIVHLDKLEEVTTEVGN-VNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQNY---FDAWQALLL 228
Cdd:cd11064  73 RALREFMESVVrEKVEKLLVPLLDHAAESGKvVDLQDVLQRFTFDVICKIAFGVDPGSLSPSLPEVPFakaFDDASEAVA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   229 K----PDIFFKI-SWLC----KKYEEAAKDLKG-AMEILIEQKRQKLSTVEKLDEHMDFASQLIFA--QNRGDLTAENVN 296
Cdd:cd11064 153 KrfivPPWLWKLkRWLNigseKKLREAIRVIDDfVYEVISRRREELNSREEENNVREDLLSRFLASeeEEGEPVSDKFLR 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   297 QCVLEMMIAAPDTLSVTL--FIMLIliADDPTVEEKMMREIETVMGDREVQS------DDMPNLKIVENFIYESMRYQPV 368
Cdd:cd11064 233 DIVLNFILAGRDTTAAALtwFFWLL--SKNPRVEEKIREELKSKLPKLTTDEsrvptyEELKKLVYLHAALSESLRLYPP 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   369 VDLIMRKALQDDVI-DGYPVKKGTNIILNI---GRMHK------LEFfpKPNEF-SLENFEKNVPSRYFQPFGFGPRGCV 437
Cdd:cd11064 311 VPFDSKEAVNDDVLpDGTFVKKGTRIVYSIyamGRMESiwgedaLEF--KPERWlDEDGGLRPESPYKFPAFNAGPRICL 388
                       410       420
                ....*....|....*....|....*..
gi 117292   438 GKFIAMVMMKAILVTLLRRCRVQTMKG 464
Cdd:cd11064 389 GKDLAYLQMKIVAAAILRRFDFKVVPG 415
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
78-456 1.68e-32

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: 128.79  E-value: 1.68e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    78 KTYGEFVRVWISGEETFIISKSSSVFHVM------KHWNYVSRFGSKLGLQCIGmyeNGIIFNNNPAHWKEIRPFFTKAL 151
Cdd:cd20613   9 KEYGPVFVFWILHRPIVVVSDPEAVKEVLitlnlpKPPRVYSRLAFLFGERFLG---NGLVTEVDHEKWKKRRAILNPAF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   152 SGPGLVRMIAICVESTIVHLDKLEEV---TTEVgnvNVLNLMRRIMLDTSNKLFLGVPLD-----ESAIVLKIQNYFDAW 223
Cdd:cd20613  86 HRKYLKNLMDEFNESADLLVEKLSKKadgKTEV---NMLDEFNRVTLDVIAKVAFGMDLNsiedpDSPFPKAISLVLEGI 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   224 QALLLKPDIFFKIS--WLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEhmDFASQLI-FAQNRGDLTAENVNQCVL 300
Cdd:cd20613 163 QESFRNPLLKYNPSkrKYRREVREAIKFLRETGRECIEERLEALKRGEEVPN--DILTHILkASEEEPDFDMEELLDDFV 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   301 EMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDRE-VQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQD 379
Cdd:cd20613 241 TFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQyVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKD 320
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   380 DVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENFEKNVPSR-----YFqPFGFGPRGCVGKFIAMVMMKAILVTL 453
Cdd:cd20613 321 IELGGYKIPAGTTVLVSTYVMGRMEeYFEDPLKFDPERFSPEAPEKipsyaYF-PFSLGPRSCIGQQFAQIEAKVILAKL 399

                ...
gi 117292   454 LRR 456
Cdd:cd20613 400 LQN 402
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
132-461 1.95e-32

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: 128.49  E-value: 1.95e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   132 IFNNNPAHWKEIR-----PFFTKALSGpglvrMIAICVESTIVHLDKLEEVTTEvGNVNVLNLMRRIMLDTSNKLFLGVP 206
Cdd:cd11057  47 LFSAPYPIWKLQRkalnpSFNPKILLS-----FLPIFNEEAQKLVQRLDTYVGG-GEFDILPDLSRCTLEMICQTTLGSD 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   207 LD-------------ESAIVLKIQNYFDAWqallLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDE 273
Cdd:cd11057 121 VNdesdgneeylesyERLFELIAKRVLNPW----LHPEFIYRLTGDYKEEQKARKILRAFSEKIIEKKLQEVELESNLDS 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   274 HMD---------FASQLI-FAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGD-- 341
Cdd:cd11057 197 EEDeengrkpqiFIDQLLeLARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDdg 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   342 REVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVID-GYPVKKGTNIILNIGRMHKLEFF--PKPNEFSLENFE 418
Cdd:cd11057 277 QFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSnGVVIPKGTTIVIDIFNMHRRKDIwgPDADQFDPDNFL 356
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 117292   419 -KNVPSRY---FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQT 461
Cdd:cd11057 357 pERSAQRHpyaFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKT 403
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
139-461 1.18e-29

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: 120.38  E-value: 1.18e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   139 HWKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDES-----AIV 213
Cdd:cd11055  59 RWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQnnpddPFL 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   214 LKIQNYFDAWQ-----ALLLKPDIFFKISWL-CKKYEEAAKDLKGAMEILIEQKRQKLSTVEKldehmDFASQLIFAQNR 287
Cdd:cd11055 139 KAAKKIFRNSIirlflLLLLFPLRLFLFLLFpFVFGFKSFSFLEDVVKKIIEQRRKNKSSRRK-----DLLQLMLDAQDS 213
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   288 GD------LTA-ENVNQCVLeMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQS-DDMPNLKIVENFI 359
Cdd:cd11055 214 DEdvskkkLTDdEIVAQSFI-FLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTyDTVSKLKYLDMVI 292
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   360 YESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF---EKNVPSRY-FQPFGFGPR 434
Cdd:cd11055 293 NETLRLYPPAFFISRECKEDCTINGVFIPKGVDVVIPVYAIHHdPEFWPDPEKFDPERFspeNKAKRHPYaYLPFGAGPR 372
                       330       340
                ....*....|....*....|....*..
gi 117292   435 GCVGKFIAMVMMKAILVTLLRRCRVQT 461
Cdd:cd11055 373 NCIGMRFALLEVKLALVKILQKFRFVP 399
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
124-468 3.49e-29

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: 119.20  E-value: 3.49e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   124 IGMYENGIIFNNNPAHWKEIRPFFTKALSGP---------------GLVRMIAICVES-TIVHL-DKLEEVTtevgnvnv 186
Cdd:cd20618  45 FSYNGQDIVFAPYGPHWRHLRKICTLELFSAkrlesfqgvrkeelsHLVKSLLEESESgKPVNLrEHLSDLT-------- 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   187 LNLMRRIMLdtsNKLFLGVPLDESAIVLKIQNYFDAWQALLLKPDI--------FFKISWLCKKYEEAAKDLKGAMEILI 258
Cdd:cd20618 117 LNNITRMLF---GKRYFGESEKESEEAREFKELIDEAFELAGAFNIgdyipwlrWLDLQGYEKRMKKLHAKLDRFLQKII 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   259 EQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTL-FIMLILIaDDPTVEEKMMREIET 337
Cdd:cd20618 194 EEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLDMLAAGTDTSAVTIeWAMAELL-RHPEVMRKAQEELDS 272
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   338 VMG-DREVQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILN---IGRMHKLefFPKPNEF 412
Cdd:cd20618 273 VVGrERLVEESDLPKLPYLQAVVKETLRLHPPGPLlLPHESTEDCKVAGYDIPAGTRVLVNvwaIGRDPKV--WEDPLEF 350
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 117292   413 S----LENFEKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKAILVTLLRRC--RVQTMKGRGLN 468
Cdd:cd20618 351 KperfLESDIDDVKGQDFEllPFGSGRRMCPGMPLGLRMVQLTLANLLHGFdwSLPGPKPEDID 414
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
190-465 4.25e-29

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: 118.90  E-value: 4.25e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   190 MRRIMLDTSNKLFLGVPLDESAIV-----LKIQNYFDAWQALLLKpdiffkisWLCK-------KYEEAAKDLKGAMEIL 257
Cdd:cd11049 116 MHRLTLRVVARTLFSTDLGPEAAAelrqaLPVVLAGMLRRAVPPK--------FLERlptpgnrRFDRALARLRELVDEI 187
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   258 IEQKRqklstvEKLDEHMDFASQLIFA--QNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREI 335
Cdd:cd11049 188 IAEYR------ASGTDRDDLLSLLLAArdEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAEL 261
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   336 ETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFS- 413
Cdd:cd11049 262 DAVLGGRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVELGGHRLPAGTEVAFSPYALHRDpEVYPDPERFDp 341
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 117292   414 ---LENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGR 465
Cdd:cd11049 342 drwLPGRAAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGR 396
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
74-458 1.37e-28

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


Pssm-ID: 410675 [Multi-domain]  Cd Length: 427  Bit Score: 117.44  E-value: 1.37e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    74 NYYNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWN-YVSRFGSKLGLQciGMYENGIIFNNNPaHWKEIRPFFTKALS 152
Cdd:cd11052   5 YHWIKQYGKNFLYWYGTDPRLYVTEPELIKELLSKKEgYFGKSPLQPGLK--KLLGRGLVMSNGE-KWAKHRRIANPAFH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   153 GPGLVRMIAICVESTIVHLDKLEEVTTEVGN-VNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQnyfDAWQALLLKP- 230
Cdd:cd11052  82 GEKLKGMVPAMVESVSDMLERWKKQMGEEGEeVDVFEEFKALTADIISRTAFGSSYEEGKEVFKLL---RELQKICAQAn 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   231 -DIFFKIS-WLCKKYEEAAKDLKGAMEIL----IEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDltaENVNQCVLEMM- 303
Cdd:cd11052 159 rDVGIPGSrFLPTKGNKKIKKLDKEIEDSlleiIKKREDSLKMGRGDDYGDDLLGLLLEANQSDD---QNKNMTVQEIVd 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   304 ------IAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMR-YQPVVDLImRKA 376
Cdd:cd11052 236 ecktffFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPSDSLSKLKTVSMVINESLRlYPPAVFLT-RKA 314
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   377 LQDDVIDGYPVKKGTNIILNIGRMHKLEFF--PKPNEFSLENFEKNVP-----SRYFQPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd11052 315 KEDIKLGGLVIPKGTSIWIPVLALHHDEEIwgEDANEFNPERFADGVAkaakhPMAFLPFGLGPRNCIGQNFATMEAKIV 394

                ....*....
gi 117292   450 LVTLLRRCR 458
Cdd:cd11052 395 LAMILQRFS 403
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
128-464 1.59e-28

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: 116.90  E-value: 1.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   128 ENGIIFNNNPAHwKEIRPFFTKALSGPGL-VRMIAICVESTIVHLDKLeevtTEVGNVNVLNLMRRIMLDTSNKLFLGvp 206
Cdd:cd11043  52 KSSLLTVSGEEH-KRLRGLLLSFLGPEALkDRLLGDIDELVRQHLDSW----WRGKSVVVLELAKKMTFELICKLLLG-- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   207 LDESAIVLKIQNYFDAW-QALLLKP-DIFFKISWLCKKyeeAAKDLKGAMEILIEQKRQKLSTVEkldEHMDFASQLIFA 284
Cdd:cd11043 125 IDPEEVVEELRKEFQAFlEGLLSFPlNLPGTTFHRALK---ARKRIRKELKKIIEERRAELEKAS---PKGDLLDVLLEE 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   285 QNRGD--LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMRE----IETVMGDREVQSDDMPNLKIVENF 358
Cdd:cd11043 199 KDEDGdsLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeiAKRKEEGEGLTWEDYKSMKYTWQV 278
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   359 IYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENFEKN--VPSRYFQPFGFGPRG 435
Cdd:cd11043 279 INETLRLAPIVPGVFRKALQDVEYKGYTIPKGWKVLWSARATHLdPEYFPDPLKFNPWRWEGKgkGVPYTFLPFGGGPRL 358
                       330       340
                ....*....|....*....|....*....
gi 117292   436 CVGKFIAMVMMKAILVTLLRRCRVQTMKG 464
Cdd:cd11043 359 CPGAELAKLEILVFLHHLVTRFRWEVVPD 387
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
136-456 3.67e-28

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: 116.60  E-value: 3.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   136 NPAHWKEIRP-FFTKALSgpgLVRMIAicvestivhlDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDesAIVL 214
Cdd:cd11069  73 SYRHVKELYPiFWSKAEE---LVDKLE----------EEIEESGDESISIDVLEWLSRATLDIIGLAGFGYDFD--SLEN 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   215 KIQNYFDAWQALL----LKPDIFFKISWL------------CKKYEEAAKDLKGAMEILIEQKRQKLsTVEKLDEHMDFA 278
Cdd:cd11069 138 PDNELAEAYRRLFeptlLGSLLFILLLFLprwlvrilpwkaNREIRRAKDVLRRLAREIIREKKAAL-LEGKDDSGKDIL 216
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   279 SQLI----FAQNRGDLTAENVNQcVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETV---MGDREVQSDDMPN 351
Cdd:cd11069 217 SILLrandFADDERLSDEELIDQ-ILTFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAAlpdPPDGDLSYDDLDR 295
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   352 LKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKLEFF--PKPNEF-------SLENFEKNVP 422
Cdd:cd11069 296 LPYLNAVCRETLRLYPPVPLTSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIwgPDAEEFnperwlePDGAASPGGA 375
                       330       340       350
                ....*....|....*....|....*....|....*.
gi 117292   423 SRY--FQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11069 376 GSNyaLLTFLHGPRSCIGKKFALAEMKVLLAALVSR 411
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
79-480 1.09e-26

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: 112.07  E-value: 1.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    79 TYGEFVRVWISGEETFIISKSSSVFHVMKhwnyvsrfgSKLGLQ-CIGM-YE-------NGIIFNNNPAhWKEIRpfftK 149
Cdd:cd11046   9 EYGPIYKLAFGPKSFLVISDPAIAKHVLR---------SNAFSYdKKGLlAEilepimgKGLIPADGEI-WKKRR----R 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   150 ALSgPGL--------VRMIAICVESTIvhlDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFL----GVPLDESAIVLKIQ 217
Cdd:cd11046  75 ALV-PALhkdylemmVRVFGRCSERLM---EKLDAAAETGESVDMEEEFSSLTLDIIGLAVFnydfGSVTEESPVIKAVY 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   218 N-YFDA-----WQALLLKPDIFFKISWLCKKYEEAAKDLKGAMEILIeQKRQKLSTVEKLD-EHMDF-----ASQLIF-A 284
Cdd:cd11046 151 LpLVEAehrsvWEPPYWDIPAALFIVPRQRKFLRDLKLLNDTLDDLI-RKRKEMRQEEDIElQQEDYlneddPSLLRFlV 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   285 QNRG-DLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDR-EVQSDDMPNLKIVENFIYES 362
Cdd:cd11046 230 DMRDeDVDSKQLRDDLMTMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRlPPTYEDLKKLKYTRRVLNES 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   363 MRYQPVVDLIMRKALQDDVIDG--YPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENFE---KNVPSRY-----FQPFGF 431
Cdd:cd11046 310 LRLYPQPPVLIRRAVEDDKLPGggVKVPAGTDIFISVYNLHRSpELWEDPEEFDPERFLdpfINPPNEViddfaFLPFGG 389
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 117292   432 GPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKGRGlnniqknnDLSMHP 480
Cdd:cd11046 390 GPRKCLGDQFALLEATVALAMLLRRFDFELDVGPR--------HVGMTT 430
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
141-458 5.08e-26

cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate cytochrome P450 family 26 enzymes, and similar cytochrome P450s; This family includes cyanobacterial CYP120A1 and vertebrate cytochrome P450s 26A1 (CYP26A1), 26B1 (CYP26B1), and 26C1 (CYP26C1). These are retinoic acid-metabolizing cytochromes that play key roles in retinoic acid (RA) metabolism. Human and zebrafish CYP26a1, as well as Synechocystis CYP120A1 are characterized as RA hydroxylases. RA is a critical signaling molecule that regulates gene transcription and the cell cycle. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410670 [Multi-domain]  Cd Length: 420  Bit Score: 110.07  E-value: 5.08e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   141 KEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVttevGNVNVLNLMRRIMLDTSNKLFLGvpLDESAIVLKIQNYF 220
Cdd:cd11044  80 RRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLKA----GEVALYPELRRLTFDVAARLLLG--LDPEVEAEALSQDF 153
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   221 DAW-QALL-LKPDIFFKiswLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKldehmDFASQLIFAQ-NRG-DLTAENVN 296
Cdd:cd11044 154 ETWtDGLFsLPVPLPFT---PFGRAIRARNKLLARLEQAIRERQEEENAEAK-----DALGLLLEAKdEDGePLSMDELK 225
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   297 QCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKA 376
Cdd:cd11044 226 DQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPVGGGFRKV 305
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   377 LQDDVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENF------EKNVPSRYFqPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd11044 306 LEDFELGGYQIPKGWLVYYSIRDTHRDpELYPDPERFDPERFsparseDKKKPFSLI-PFGGGPRECLGKEFAQLEMKIL 384

                ....*....
gi 117292   450 LVTLLRRCR 458
Cdd:cd11044 385 ASELLRNYD 393
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
81-456 9.09e-26

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: 109.33  E-value: 9.09e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    81 GEFVRVWISGEETFIISKSSSVFHVMKH----WNYVSRFGSKLGLQCIgmyeNGIiFNNNPAHWKEIRPFFTKALSGPGL 156
Cdd:cd11083   1 GSAYRFRLGRQPVLVISDPELIREVLRRrpdeFRRISSLESVFREMGI----NGV-FSAEGDAWRRQRRLVMPAFSPKHL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   157 VRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGV----------PLDES------AIVLKIQNYF 220
Cdd:cd11083  76 RYFFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYdlntlerggdPLQEHlervfpMLNRRVNAPF 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   221 DAWQALLLKPDiffkiswlcKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQN--RGDLTAENVNQC 298
Cdd:cd11083 156 PYWRYLRLPAD---------RALDRALVEVRALVLDIIAAARARLAANPALAEAPETLLAMMLAEDdpDARLTDDEIYAN 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   299 VLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQ--SDDMPNLKIVENFIYESMRYQPVVDLIMRKA 376
Cdd:cd11083 227 VLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPplLEALDRLPYLEAVARETLRLKPVAPLLFLEP 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   377 LQDDVIDGYPVKKGTNIIL---NIGRmhKLEFFPKPNEFSLENFEKNVPSRY------FQPFGFGPRGCVGKFIAMVMMK 447
Cdd:cd11083 307 NEDTVVGDIALPAGTPVFLltrAAGL--DAEHFPDPEEFDPERWLDGARAAEphdpssLLPFGAGPRLCPGRSLALMEMK 384

                ....*....
gi 117292   448 AILVTLLRR 456
Cdd:cd11083 385 LVFAMLCRN 393
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
227-465 2.40e-25

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: 108.12  E-value: 2.40e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   227 LLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMD------------FASQLIFA-QNRGDLTAE 293
Cdd:cd20660 152 WLWPDFIYSLTPDGREHKKCLKILHGFTNKVIQERKAELQKSLEEEEEDDedadigkrkrlaFLDLLLEAsEEGTKLSDE 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   294 NVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGD--REVQSDDMPNLKIVENFIYESMRYQPVVDL 371
Cdd:cd20660 232 DIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDsdRPATMDDLKEMKYLECVIKEALRLFPSVPM 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   372 IMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRGCVGKFIAMVMM 446
Cdd:cd20660 312 FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRdPRQFPDPEKFDPDRFlPENSAGRHpyaYIPFSAGPRNCIGQKFALMEE 391
                       250
                ....*....|....*....
gi 117292   447 KAILVTLLRRCRVQTMKGR 465
Cdd:cd20660 392 KVVLSSILRNFRIESVQKR 410
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
231-454 4.62e-25

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


Pssm-ID: 410747  Cd Length: 447  Bit Score: 107.32  E-value: 4.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   231 DIFFKISWL-CKKYEEA----AKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGDLTAEN-----VNQCVL 300
Cdd:cd20654 168 DAIPFLGWLdFGGHEKAmkrtAKELDSILEEWLEEHRQKRSSSGKSKNDEDDDDVMMLSILEDSQISGYdadtvIKATCL 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   301 EMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG-DREVQSDDMPNLKIVENFIYESMR-YQPVVDLIMRKALQ 378
Cdd:cd20654 248 ELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGkDRWVEESDIKNLVYLQAIVKETLRlYPPGPLLGPREATE 327
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   379 DDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLENFEKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKA 448
Cdd:cd20654 328 DCTVGGYHVPKGTRLLVNVWKIQRdpnvwsdpLEF--KPERFLTTHKDIDVRGQNFEliPFGSGRRSCPGVSFGLQVMHL 405

                ....*.
gi 117292   449 ILVTLL 454
Cdd:cd20654 406 TLARLL 411
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
108-455 1.02e-24

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: 106.19  E-value: 1.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   108 HWNYVSRFGSKLGLQCIGmyeNGIIFNNNPAhWKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVttevgNVNVL 187
Cdd:cd20621  31 HHYYKKKFGPLGIDRLFG---KGLLFSEGEE-WKKQRKLLSNSFHFEKLKSRLPMINEITKEKIKKLDNQ-----NVNII 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   188 NLMRRIMLDTSNKLFLGVPLDE---------SAIVLKIQNYFDAW---------QALLLKPDIFFKISWLCKKYEEAAKD 249
Cdd:cd20621 102 QFLQKITGEVVIRSFFGEEAKDlkingkeiqVELVEILIESFLYRfsspyfqlkRLIFGRKSWKLFPTKKEKKLQKRVKE 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   250 LKGAMEILIEQKR---QKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPT 326
Cdd:cd20621 182 LRQFIEKIIQNRIkqiKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPE 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   327 VEEKMMREIETVMGD-REVQSDDMPNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNI-ILNIGRMHKL 403
Cdd:cd20621 262 IQEKLRQEIKSVVGNdDDITFEDLQKLNYLNAFIKEVLRLYNPAPfLFPRVATQDHQIGDLKIKKGWIVnVGYIYNHFNP 341
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 117292   404 EFFPKPNEFS----LENFEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20621 342 KYFENPDEFNperwLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYILK 397
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
125-456 4.73e-24

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  Cd Length: 441  Bit Score: 104.30  E-value: 4.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   125 GMYENGIIFNNNPAHWKEIRPFFTKALsgPGLVRMIAicvESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLG 204
Cdd:cd11041  54 GFGTGGSVVLDSPLHVDVVRKDLTPNL--PKLLPDLQ---EELRAALDEELGSCTEWTEVNLYDTVLRIVARVSARVFVG 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   205 VPL-DESAIVLKIQNY----FDAWQALLLKPDIFFKI-SWL---CKKYEeaaKDLKGAMEILIE--QKRQKLSTVEKLDE 273
Cdd:cd11041 129 PPLcRNEEWLDLTINYtidvFAAAAALRLFPPFLRPLvAPFlpePRRLR---RLLRRARPLIIPeiERRRKLKKGPKEDK 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   274 HMDFASQLI-FAQNRGDLTAENVNQCVLEMMIAAPDTLSVTL-FIMLILIADDPTVEEkmMR-EIETVMGDREVQSDD-M 349
Cdd:cd11041 206 PNDLLQWLIeAAKGEGERTPYDLADRQLALSFAAIHTTSMTLtHVLLDLAAHPEYIEP--LReEIRSVLAEHGGWTKAaL 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   350 PNLKIVENFIYESMRYQPVVDLIM-RKALQDDVI-DGYPVKKGTNIILNIGRMHKLE-FFPKPNEF---------SLENF 417
Cdd:cd11041 284 NKLKKLDSFMKESQRLNPLSLVSLrRKVLKDVTLsDGLTLPKGTRIAVPAHAIHRDPdIYPDPETFdgfrfyrlrEQPGQ 363
                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 117292   418 EKN----VPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11041 364 EKKhqfvSTSPDFLGFGHGRHACPGRFFASNEIKLILAHLLLN 406
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
184-460 7.38e-24

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: 103.43  E-value: 7.38e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   184 VNVLNLMRRIMLDTSNKLFLGVplDESAIVLKIQNYFDAWQALLLKPDIFFK------ISWL-CKKYEEAAKDLKGAMEI 256
Cdd:cd11053 111 FDLRELMQEITLEVILRVVFGV--DDGERLQELRRLLPRLLDLLSSPLASFPalqrdlGPWSpWGRFLRARRRIDALIYA 188
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   257 LIEQKRQKlstvekldehmdfasqliFAQNRGDltaenvnqcVLEMMIAAPD----TLS--------VTLFI-------- 316
Cdd:cd11053 189 EIAERRAE------------------PDAERDD---------ILSLLLSARDedgqPLSdeelrdelMTLLFaghettat 241
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   317 ----MLILIADDPTVEEKMMREIETVMGDREvqSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTN 392
Cdd:cd11053 242 alawAFYWLHRHPEVLARLLAELDALGGDPD--PEDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVELGGYTLPAGTT 319
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   393 IILNIGRMHKLE-FFPKPNEFSLENFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQ 460
Cdd:cd11053 320 VAPSIYLTHHRPdLYPDPERFRPERFLGRKPSPYeYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLE 389
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
241-461 7.62e-24

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: 103.77  E-value: 7.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   241 KKYEEAAKDLkgaMEILIEQKRQKLSTVEKLDEHMDFasqlifaqnrGDLTAenvnQCVLeMMIAAPDTLSVTLFIMLIL 320
Cdd:cd11056 194 EKNNIVRNDF---IDLLLELKKKGKIEDDKSEKELTD----------EELAA----QAFV-FFLAGFETSSSTLSFALYE 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   321 IADDPTVEEKMMREIETVM--GDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDG--YPVKKGTNIILN 396
Cdd:cd11056 256 LAKNPEIQEKLREEIDEVLekHGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGtdVVIEKGTPVIIP 335
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   397 IGRMHKL-EFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQT 461
Cdd:cd11056 336 VYALHHDpKYYPEPEKFDPERFsPENKKKRHpytYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEP 405
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
226-459 9.40e-24

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: 103.40  E-value: 9.40e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   226 LLLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTvEKLDE-----HMDFASQLIFAQNR-GD-LTAENVNQC 298
Cdd:cd20659 153 PLLHFDWIYYLTPEGRRFKKACDYVHKFAEEIIKKRRKELED-NKDEAlskrkYLDFLDILLTARDEdGKgLTDEEIRDE 231
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   299 VLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDR-EVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKAL 377
Cdd:cd20659 232 VDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRdDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLT 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   378 QDDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLENFeKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAI 449
Cdd:cd20659 312 KPITIDGVTLPAGTLIAINIYALHHnptvwedpEEF--DPERFLPENI-KKRDPFAFIPFSAGPRNCIGQNFAMNEMKVV 388
                       250
                ....*....|
gi 117292   450 LVTLLRRCRV 459
Cdd:cd20659 389 LARILRRFEL 398
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
229-456 2.03e-23

cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome P450/NADPH--P450 reductase; Cytochrome P450 102A1, also called cytochrome P450(BM-3) or P450BM-3, is a bifunctional cytochrome P450/NADPH--P450 reductase. These proteins fuse an N-terminal cytochrome p450 with a C-terminal cytochrome p450 reductase (CYPOR). It functions as a fatty acid monooxygenase, catalyzing the hydroxylation of fatty acids at omega-1, omega-2 and omega-3 positions, with activity towards fatty acids with a chain length of 9-18 carbons. Its NADPH-dependent reductase activity (via the C-terminal domain) allows electron transfer from NADPH to the heme iron of the N-terminal cytochrome P450. CYP120A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 102.26  E-value: 2.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   229 KPDIFFKISWLCK-KYEEAAKDLKGAMEILIEQkRQKLSTVEKLD--EHMDFASQlifAQNRGDLTAENVNQCVLEMMIA 305
Cdd:cd11068 166 RPPILNKLRRRAKrQFREDIALMRDLVDEIIAE-RRANPDGSPDDllNLMLNGKD---PETGEKLSDENIRYQMITFLIA 241
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   306 APDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDG- 384
Cdd:cd11068 242 GHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLGDDPPPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGk 321
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   385 YPVKKGTNIILNIGRMHK---------LEFfpKPNEFSLENFEKnVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd11068 322 YPLKKGDPVLVLLPALHRdpsvwgedaEEF--RPERFLPEEFRK-LPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQ 398

                .
gi 117292   456 R 456
Cdd:cd11068 399 R 399
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
130-456 2.85e-23

cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This subfamily is composed of insect and crustacean cytochrome P450s including Diploptera punctata cytochrome P450 15A1 (CYP15A1 or CYP15A1), Panulirus argus CYP2L1, and CYP303A1, CYP304A1, and CYP305A1 from Drosophila melanogaster. CYP15A1, also called methyl farnesoate epoxidase, catalyzes the conversion of methyl farnesoate to juvenile hormone III acid during juvenile hormone biosynthesis. CYP303A1, CYP304A1, and CYP305A1 may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. The CYP15A1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410744 [Multi-domain]  Cd Length: 423  Bit Score: 101.91  E-value: 2.85e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   130 GIIFNNNPaHWKEIRPFFTKALS--GPGLVRMIAICVEST---IVHLDKLEEVTTEVGNV------NVLNLM---RRIML 195
Cdd:cd20651  50 GITFTDGP-FWKEQRRFVLRHLRdfGFGRRSMEEVIQEEAeelIDLLKKGEKGPIQMPDLfnvsvlNVLWAMvagERYSL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   196 DtSNKLF-LGvpldesAIVLKIQNYFDAWQALLlkpDIFFKISWLC------KKYEEAAKDLKGAMEILIEQKRQKLstv 268
Cdd:cd20651 129 E-DQKLRkLL------ELVHLLFRNFDMSGGLL---NQFPWLRFIApefsgyNLLVELNQKLIEFLKEEIKEHKKTY--- 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   269 eKLDEHMDFASQLIFAQNRGDLTAENVN--QCV---LEMMIAAPDTLSVTL-FIMLILIADdPTVEEKMMREIETVMG-D 341
Cdd:cd20651 196 -DEDNPRDLIDAYLREMKKKEPPSSSFTddQLVmicLDLFIAGSETTSNTLgFAFLYLLLN-PEVQRKVQEEIDEVVGrD 273
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   342 REVQSDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF-- 417
Cdd:cd20651 274 RLPTLDDRSKLPYTEAVILEVLRIFTLVPIgIPHRALKDTTLGGYRIPKDTTILASLYSVHMdPEYWGDPEEFRPERFld 353
                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 117292   418 --EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd20651 354 edGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQN 394
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
132-456 5.29e-23

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: 101.09  E-value: 5.29e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   132 IFNNNPAHWKE----IRPFFTKalsgpglvrmiaicveSTIVHLDKLEE--------VTTEVGNVNVLNLMRRIMLDTSN 199
Cdd:cd11063  52 IFTSDGEEWKHsralLRPQFSR----------------DQISDLELFERhvqnliklLPRDGSTVDLQDLFFRLTLDSAT 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   200 KLFLG------VPLDESAIVLKIQNYFDAWQALLLKPDIFFKISWLC--KKYEEAAKDLKGAMEILIEQ--KRQKLSTVE 269
Cdd:cd11063 116 EFLFGesvdslKPGGDSPPAARFAEAFDYAQKYLAKRLRLGKLLWLLrdKKFREACKVVHRFVDPYVDKalARKEESKDE 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   270 KLDEHMDFASQLI-FAQNRGDLTAEnvnqcVLEMMIAAPDTLSVTL-FIMLILiADDPTVEEKMMREIETVMGD-REVQS 346
Cdd:cd11063 196 ESSDRYVFLDELAkETRDPKELRDQ-----LLNILLAGRDTTASLLsFLFYEL-ARHPEVWAKLREEVLSLFGPePTPTY 269
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   347 DDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVI------DGYP---VKKGTNIILNIGRMHKLE--FFPKPNEFSLE 415
Cdd:cd11063 270 EDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLprgggpDGKSpifVPKGTRVLYSVYAMHRRKdiWGPDAEEFRPE 349
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 117292   416 NFEKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11063 350 RWEDLKRPGWeYLPFNGGPRICLGQQFALTEASYVLVRLLQT 391
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
115-463 1.01e-22

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: 100.05  E-value: 1.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   115 FGSKLGlQCIGMYengiifnnNPAHWKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTT--EVGNVNVLNLMRR 192
Cdd:cd20615  44 FGQLLG-QCVGLL--------SGTDWKRVRKVFDPAFSHSAAVYYIPQFSREARKWVQNLPTNSGdgRRFVIDPAQALKF 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   193 IMLDTSNKLFLGVPLDE------SAIVLKIQNYFDAWQALLLKpdifFKIS-WLckkYEEAAKDLKG--------AMEIL 257
Cdd:cd20615 115 LPFRVIAEILYGELSPEekeelwDLAPLREELFKYVIKGGLYR----FKISrYL---PTAANRRLREfqtrwrafNLKIY 187
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   258 -IEQKRQKLSTVEKLDEHMdfasqlifaqNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIE 336
Cdd:cd20615 188 nRARQRGQSTPIVKLYEAV----------EKGDITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIS 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   337 TVMGDREVQSDDmpnlKIVEN------FIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHKLEFFPKP 409
Cdd:cd20615 258 AAREQSGYPMED----YILSTdtllayCVLESLRLRPLLAFsVPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWGP 333
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 117292   410 N--EFSLENFEKNVPS--RY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMK 463
Cdd:cd20615 334 DgeAYRPERFLGISPTdlRYnFWRFGFGPRKCLGQHVADVILKALLAHLLEQYELKLPD 392
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
129-456 1.71e-22

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: 99.59  E-value: 1.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   129 NGIIFNNNPAHWKEIRPFFTKAL-----SGPGLVRMIAICVESTIVHLDKLEE----VTTEVGNVnVLNLMRRIMLDTSN 199
Cdd:cd11027  51 KDIAFGDYSPTWKLHRKLAHSALrlyasGGPRLEEKIAEEAEKLLKRLASQEGqpfdPKDELFLA-VLNVICSITFGKRY 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   200 KLflgvpLDESaiVLKIQNYFDAWQALLLKPDIFFKISWLcKKYE-EAAKDLKGAMEILIEQKRQKLST-VEKLDEHM-- 275
Cdd:cd11027 130 KL-----DDPE--FLRLLDLNDKFFELLGAGSLLDIFPFL-KYFPnKALRELKELMKERDEILRKKLEEhKETFDPGNir 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   276 DFASQLIFAQ----NRGD-----LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG-DREVQ 345
Cdd:cd11027 202 DLTDALIKAKkeaeDEGDedsglLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGrDRLPT 281
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   346 SDDMPNLKIVENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLEN 416
Cdd:cd11027 282 LSDRKRLPYLEATIAEVLRLSSVVPLaLPHKTTCDTTLRGYTIPKGTTVLVNLWALHHdpkewddpDEF--RPERFLDEN 359
                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 117292   417 FEKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11027 360 GKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQK 399
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
79-458 5.63e-22

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: 98.17  E-value: 5.63e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    79 TYGEfVRVWISGEETFIISKSSSVFHVMKHWNYVSRFGSKLGLqcIGMYENGIIFNNNPAhWKEIRPFFTKALSGPGLVR 158
Cdd:cd11070   1 KLGA-VKILFVSRWNILVTKPEYLTQIFRRRDDFPKPGNQYKI--PAFYGPNVISSEGED-WKRYRKIVAPAFNERNNAL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   159 MIAICVEST--IVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDES-AIVLKIQNYFDAWQALLLKPDIF-F 234
Cdd:cd11070  77 VWEESIRQAqrLIRYLLEEQPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPALdEEESSLHDTLNAIKLAIFPPLFLnF 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   235 KIS-----WLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHM--DFASQLIFAQNRGDLTAE----NVNQcvleMM 303
Cdd:cd11070 157 PFLdrlpwVLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTesVVASRLKRARRSGGLTEKellgNLFI----FF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   304 IAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQ---SDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 380
Cdd:cd11070 233 IAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDwdyEEDFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPV 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   381 VI-----DGYPVKKGTNIILNIGRMHK---------LEFFPK----PNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIA 442
Cdd:cd11070 313 VVitglgQEIVIPKGTYVGYNAYATHRdptiwgpdaDEFDPErwgsTSGEIGAATRFTPARGAFIPFSAGPRACLGRKFA 392
                       410
                ....*....|....*.
gi 117292   443 MVMMKAILVTLLRRCR 458
Cdd:cd11070 393 LVEFVAALAELFRQYE 408
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
129-454 8.37e-22

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


Pssm-ID: 410733 [Multi-domain]  Cd Length: 426  Bit Score: 97.48  E-value: 8.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   129 NGIIFNNNPaHW----KEIRP-FFTKALSGpglvrMIAICVESTIVHLDKLEEVTTEVG----NVNVLNLMRRIMLDTSN 199
Cdd:cd20640  60 GGILTSNGP-HWahqrKIIAPeFFLDKVKG-----MVDLMVDSAQPLLSSWEERIDRAGgmaaDIVVDEDLRAFSADVIS 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   200 KLFLGVPLDE-SAIVLKIQnyfdAWQALLLKPDIFFKIS---WLCKKYEEAAKDLKGAMEILIEQ---KRQKLSTVEKld 272
Cdd:cd20640 134 RACFGSSYSKgKEIFSKLR----ELQKAVSKQSVLFSIPglrHLPTKSNRKIWELEGEIRSLILEivkEREEECDHEK-- 207
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   273 ehmDFASQLIFAQNRGDL---TAEN--VNQCVlEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSD 347
Cdd:cd20640 208 ---DLLQAILEGARSSCDkkaEAEDfiVDNCK-NIYFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCKGGPPDAD 283
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   348 DMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMH--KLEFFPKPNEFSLENFEKNVPSRY 425
Cdd:cd20640 284 SLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLVVPKGVNIWVPVSTLHldPEIWGPDANEFNPERFSNGVAAAC 363
                       330       340       350
                ....*....|....*....|....*....|....
gi 117292   426 -----FQPFGFGPRGCVGKFIAMVMMKaILVTLL 454
Cdd:cd20640 364 kpphsYMPFGAGARTCLGQNFAMAELK-VLVSLI 396
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
302-459 2.49e-21

putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of Mycobacterium tuberculosis putative cytochrome P450 136 (CYP136) and similar proteins. It belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 95.85  E-value: 2.49e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   302 MMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVmGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDV 381
Cdd:cd11045 219 LMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGTLDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTE 297
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   382 IDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENF-----EKNVpSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd11045 298 VLGYRIPAGTLVAVSPGVTHYMpEYWPNPERFDPERFsperaEDKV-HRYaWAPFGGGAHKCIGLHFAGMEVKAILHQML 376

                ....*
gi 117292   455 RRCRV 459
Cdd:cd11045 377 RRFRW 381
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
290-465 2.66e-21

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: 96.37  E-value: 2.66e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   290 LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG--DREVQSDDMPNLKIVENFIYESMRYQP 367
Cdd:cd20680 239 LSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGksDRPVTMEDLKKLRYLECVIKESLRLFP 318
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   368 VVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-LEFFPKPNEFSLENF-EKNVPSRY---FQPFGFGPRGCVGKFIA 442
Cdd:cd20680 319 SVPLFARSLCEDCEIRGFKVPKGVNAVIIPYALHRdPRYFPEPEEFRPERFfPENSSGRHpyaYIPFSAGPRNCIGQRFA 398
                       170       180
                ....*....|....*....|...
gi 117292   443 MVMMKAILVTLLRRCRVQTMKGR 465
Cdd:cd20680 399 LMEEKVVLSCILRHFWVEANQKR 421
PLN02738 PLN02738
carotene beta-ring hydroxylase
140-464 4.59e-21

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 96.52  E-value: 4.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    140 WKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLD----ESAIVLK 215
Cdd:PLN02738 222 WRVRRRAIVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNYDFDslsnDTGIVEA 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    216 IQNY-----------FDAWQALLLKpdiffKISWLCKKYEEAAKDLKGAMEILIEQ-KRqkLSTVEKL---DEHMDF--A 278
Cdd:PLN02738 302 VYTVlreaedrsvspIPVWEIPIWK-----DISPRQRKVAEALKLINDTLDDLIAIcKR--MVEEEELqfhEEYMNErdP 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    279 SQLIFAQNRGD-LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVEN 357
Cdd:PLN02738 375 SILHFLLASGDdVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFPTIEDMKKLKYTTR 454
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    358 FIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK-------LEFF---------PKPNEfSLENFeknv 421
Cdd:PLN02738 455 VINESLRLYPQPPVLIRRSLENDMLGGYPIKRGEDIFISVWNLHRspkhwddAEKFnperwpldgPNPNE-TNQNF---- 529
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 117292    422 psRYFqPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKG 464
Cdd:PLN02738 530 --SYL-PFGGGPRKCVGDMFASFENVVATAMLVRRFDFQLAPG 569
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
127-455 6.79e-21

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  Cd Length: 435  Bit Score: 94.91  E-value: 6.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   127 YENGIIFNNNPAHWKEIRP-FFTKALSGPGL-----VRMIaiCVESTIVHLdklEEVTTEVGNVNV--------LNLMrr 192
Cdd:cd11073  52 HKSSIVWPPYGPRWRMLRKiCTTELFSPKRLdatqpLRRR--KVRELVRYV---REKAGSGEAVDIgraafltsLNLI-- 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   193 imldtSNKLF---LGVPLDESAIVLK--IQNYFDawqaLLLKPDI--------FFKISWLCKKYEEAAKDLKGAMEILIE 259
Cdd:cd11073 125 -----SNTLFsvdLVDPDSESGSEFKelVREIME----LAGKPNVadffpflkFLDLQGLRRRMAEHFGKLFDIFDGFID 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   260 QK-RQKLSTVEKLDEHMDFASQLIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTL-FIMLILIADdPTVEEKMMREIET 337
Cdd:cd11073 196 ERlAEREAGGDKKKDDDLLLLLDLELDSESELTRNHIKALLLDLFVAGTDTTSSTIeWAMAELLRN-PEKMAKARAELDE 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   338 VMG-DREVQSDDMPNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPVKKGTNIILN---IGRMhkleffPK---- 408
Cdd:cd11073 275 VIGkDKIVEESDISKLPYLQAVVKETLRLHPPAPlLLPRKAEEDVEVMGYTIPKGTQVLVNvwaIGRD------PSvwed 348
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 117292   409 PNEFSLENF---EKNVPSRYFQ--PFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd11073 349 PLEFKPERFlgsEIDFKGRDFEliPFGSGRRICPGLPLAERMVHLVLASLLH 400
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
290-484 1.30e-20

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  Cd Length: 430  Bit Score: 93.90  E-value: 1.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   290 LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG-DREVQSDDMPNLKIVENFIYESMRYQPV 368
Cdd:cd11028 227 LTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGrERLPRLSDRPNLPYTEAFILETMRHSSF 306
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   369 VDL-IMRKALQDDVIDGYPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENF---EKNV---PSRYFQPFGFGPRGCVGKF 440
Cdd:cd11028 307 VPFtIPHATTRDTTLNGYFIPKGTVVFVNLwSVNHDEKLWPDPSVFRPERFlddNGLLdktKVDKFLPFGAGRRRCLGEE 386
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 117292   441 IAMVMMKAILVTLLRRCRVQTMKGRGLNNIQKNNdLSMHPIERQ 484
Cdd:cd11028 387 LARMELFLFFATLLQQCEFSVKPGEKLDLTPIYG-LTMKPKPFK 429
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
289-461 1.84e-20

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: 93.83  E-value: 1.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   289 DLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQS-DDMPNLKIVENFIYESMRYQP 367
Cdd:cd20647 232 ELTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTaEDVPKLPLIRALLKETLRLFP 311
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   368 VVDLIMRKALQDDVIDGYPVKKGTNIIL-NIGRMHKLEFFPKPNEFSlenfeknvPSRYFQ-------------PFGFGP 433
Cdd:cd20647 312 VLPGNGRVTQDDLIVGGYLIPKGTQLALcHYSTSYDEENFPRAEEFR--------PERWLRkdaldrvdnfgsiPFGYGI 383
                       170       180
                ....*....|....*....|....*...
gi 117292   434 RGCVGKFIAMVMMKAILVTLLRRCRVQT 461
Cdd:cd20647 384 RSCIGRRIAELEIHLALIQLLQNFEIKV 411
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
293-456 2.66e-20

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  Cd Length: 425  Bit Score: 93.01  E-value: 2.66e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   293 ENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG-DREVQSDDMPNLKIVENFIYESMRYQPVVDL 371
Cdd:cd11026 225 ENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGrNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPL 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   372 -IMRKALQDDVIDGYPVKKGTNIILNIGRMHKLE-FFPKPNEFSLENF-------EKNvpsRYFQPFGFGPRGCVGKFIA 442
Cdd:cd11026 305 gVPHAVTRDTKFRGYTIPKGTTVIPNLTSVLRDPkQWETPEEFNPGHFldeqgkfKKN---EAFMPFSAGKRVCLGEGLA 381
                       170
                ....*....|....
gi 117292   443 MVMMKAILVTLLRR 456
Cdd:cd11026 382 RMELFLFFTSLLQR 395
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
233-454 4.09e-20

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: 92.53  E-value: 4.09e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   233 FFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLIFAQNRGD--LTAENVNQCVLEMMIAAPDTL 310
Cdd:cd11072 165 IDLLTGLDRKLEKVFKELDAFLEKIIDEHLDKKRSKDEDDDDDDLLDLRLQKEGDLEfpLTRDNIKAIILDMFLAGTDTS 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   311 SVTL-FIMLILIADdPTVEEKMMREIETVMGD-REVQSDDMPNLKIVENFIYESMRYQPVVD-LIMRKALQDDVIDGYPV 387
Cdd:cd11072 245 ATTLeWAMTELIRN-PRVMKKAQEEVREVVGGkGKVTEEDLEKLKYLKAVIKETLRLHPPAPlLLPRECREDCKINGYDI 323
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117292   388 KKGTNIILN---IGRMHKLefFPKPNEFSLENFEkNVPSRY----FQ--PFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd11072 324 PAKTRVIVNawaIGRDPKY--WEDPEEFRPERFL-DSSIDFkgqdFEliPFGAGRRICPGITFGLANVELALANLL 396
PLN02655 PLN02655
ent-kaurene oxidase
231-468 1.21e-19

ent-kaurene oxidase


Pssm-ID: 215354  Cd Length: 466  Bit Score: 91.34  E-value: 1.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    231 DIFFKISWLCKKYEEA---AKDLK--GAMEILIEQKRQKLSTVEKLDEHMDFASQlifaqNRGDLTAENVNQCVLEMMIA 305
Cdd:PLN02655 199 DFFPYLSWIPNKSFETrvqTTEFRrtAVMKALIKQQKKRIARGEERDCYLDFLLS-----EATHLTDEQLMMLVWEPIIE 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    306 APDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMR-YQPVVDLIMRKALQDDVIDG 384
Cdd:PLN02655 274 AADTTLVTTEWAMYELAKNPDKQERLYREIREVCGDERVTEEDLPNLPYLNAVFHETLRkYSPVPLLPPRFVHEDTTLGG 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    385 YPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENF---EKNVPSRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRV 459
Cdd:PLN02655 354 YDIPAGTQIAINIyGCNMDKKRWENPEEWDPERFlgeKYESADMYkTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFEW 433

                 ....*....
gi 117292    460 QTMKGRGLN 468
Cdd:PLN02655 434 RLREGDEEK 442
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
277-443 1.38e-19

cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus cytochrome P450 64 (CYP64), also called O-methylsterigmatocystin (OMST) oxidoreductase or aflatoxin B synthase or aflatoxin biosynthesis protein Q, and similar fungal cytochrome P450s. CYP64 converts OMST to aflatoxin B1 and converts dihydro-O-methylsterigmatocystin (DHOMST) to aflatoxin B2 in the aflatoxin biosynthesis pathway. The CYP64-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410688 [Multi-domain]  Cd Length: 425  Bit Score: 90.71  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   277 FASQLIFAQ-NRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMG-DREVQSDDMPNLKI 354
Cdd:cd11065 205 FVKDLLEELdKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGpDRLPTFEDRPNLPY 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   355 VENFIYESMRYQPVVDL-IMRKALQDDVIDGYPVKKGTNIILNI-GRMHKLEFFPKPNEFSLENFEKN------VPSRYF 426
Cdd:cd11065 285 VNAIVKEVLRWRPVAPLgIPHALTEDDEYEGYFIPKGTTVIPNAwAIHHDPEVYPDPEEFDPERYLDDpkgtpdPPDPPH 364
                       170
                ....*....|....*..
gi 117292   427 QPFGFGPRGCVGKFIAM 443
Cdd:cd11065 365 FAFGFGRRICPGRHLAE 381
PLN02290 PLN02290
cytokinin trans-hydroxylase
76-458 2.26e-19

cytokinin trans-hydroxylase


Pssm-ID: 215164  Cd Length: 516  Bit Score: 91.03  E-value: 2.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292     76 YNKTYGEFVRVWISGEETFIISKSSSVFHVMKHWNYVS------RFGSKlglQCIGmyeNGIIFNNNpAHWKEIRPFFTK 149
Cdd:PLN02290  89 WSKQYGKRFIYWNGTEPRLCLTETELIKELLTKYNTVTgkswlqQQGTK---HFIG---RGLLMANG-ADWYHQRHIAAP 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    150 ALSGPGLVRMIAICVESTIVHLDKLEEVTTEVGN-VNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQNYFDAWQALLL 228
Cdd:PLN02290 162 AFMGDRLKGYAGHMVECTKQMLQSLQKAVESGQTeVEIGEYMTRLTADIISRTEFDSSYEKGKQIFHLLTVLQRLCAQAT 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    229 KPDIFFKISWLCKKYEEAAKDLKGAME-ILIE--QKRQKLSTVEKLDEH-MDFASQLIfaqNRGDLTAENVNQCVLEMMI 304
Cdd:PLN02290 242 RHLCFPGSRFFPSKYNREIKSLKGEVErLLMEiiQSRRDCVEIGRSSSYgDDLLGMLL---NEMEKKRSNGFNLNLQLIM 318
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    305 --------AAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKA 376
Cdd:PLN02290 319 decktfffAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCGGETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMA 398
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    377 LQDDVIDGYPVKKGTNIILNIGRMHKLE--FFPKPNEFSLENF--EKNVPSRYFQPFGFGPRGCVGKFIAMVMMKAILVT 452
Cdd:PLN02290 399 FEDIKLGDLHIPKGLSIWIPVLAIHHSEelWGKDANEFNPDRFagRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAM 478

                 ....*.
gi 117292    453 LLRRCR 458
Cdd:PLN02290 479 LISKFS 484
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
140-456 2.74e-19

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: 90.20  E-value: 2.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   140 WKEIRPFFTKALSGPGLVRMIAICVESTIVHLDKLEEVTT--EVGNVNVLNLMRRIMLDTSNKLFLGVPLDESAIVLKIQ 217
Cdd:cd20639  69 WAHHRRVITPAFHMENLKRLVPHVVKSVADMLDKWEAMAEagGEGEVDVAEWFQNLTEDVISRTAFGSSYEDGKAVFRLQ 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   218 NyfdawQALLLKPDIFFKI---------------SWlckKYEeaaKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQLI 282
Cdd:cd20639 149 A-----QQMLLAAEAFRKVyipgyrflptkknrkSW---RLD---KEIRKSLLKLIERRQTAADDEKDDEDSKDLLGLMI 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   283 FAQNRGDLTAENVNQCVLE---MMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQS-DDMPNLKIVENF 358
Cdd:cd20639 218 SAKNARNGEKMTVEEIIEEcktFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTkDHLPKLKTLGMI 297
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   359 IYESMR-YQPVVDLImRKALQDDVIDGYPVKKGTNIILNIGRMH--KLEFFPKPNEFSLENFEKNVPSRY-----FQPFG 430
Cdd:cd20639 298 LNETLRlYPPAVATI-RRAKKDVKLGGLDIPAGTELLIPIMAIHhdAELWGNDAAEFNPARFADGVARAAkhplaFIPFG 376
                       330       340
                ....*....|....*....|....*.
gi 117292   431 FGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd20639 377 LGPRTCVGQNLAILEAKLTLAVILQR 402
PLN02936 PLN02936
epsilon-ring hydroxylase
233-484 2.88e-19

epsilon-ring hydroxylase


Pssm-ID: 178524  Cd Length: 489  Bit Score: 90.24  E-value: 2.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    233 FFKISWLCK------KYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFA-----SQLIF-AQNRGDLTAENVNQCVL 300
Cdd:PLN02936 205 YWKVDFLCKisprqiKAEKAVTVIRETVEDLVDKCKEIVEAEGEVIEGEEYVndsdpSVLRFlLASREEVSSVQLRDDLL 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    301 EMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 380
Cdd:PLN02936 285 SMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVED 364
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    381 VI-DGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENF--------EKNVPSRYFqPFGFGPRGCVGKFIAMVMMKAIL 450
Cdd:PLN02936 365 VLpGGYKVNAGQDIMISVYNIHRSpEVWERAEEFVPERFdldgpvpnETNTDFRYI-PFSGGPRKCVGDQFALLEAIVAL 443
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 117292    451 VTLLRRCRVQTMKGRGLN-----NIQKNNDLSMHPIERQ 484
Cdd:PLN02936 444 AVLLQRLDLELVPDQDIVmttgaTIHTTNGLYMTVSRRR 482
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
302-460 3.32e-19

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: 89.58  E-value: 3.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   302 MMI----AAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDRE--VQSDDMPNLKIVENFIYESMRYQPVVDLIMRK 375
Cdd:cd11042 216 LLIallfAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDdpLTYDVLKEMPLLHACIKETLRLHPPIHSLMRK 295
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   376 ALQD--DVIDGYPVKKGTNIILNIGRMHKL-EFFPKPNEFSLENFEKNVP------SRYFQPFGFGPRGCVGKFIAMVMM 446
Cdd:cd11042 296 ARKPfeVEGGGYVIPKGHIVLASPAVSHRDpEIFKNPDEFDPERFLKGRAedskggKFAYLPFGAGRHRCIGENFAYLQI 375
                       170
                ....*....|....
gi 117292   447 KAILVTLLRRCRVQ 460
Cdd:cd11042 376 KTILSTLLRNFDFE 389
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
253-464 7.07e-19

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: 88.79  E-value: 7.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   253 AMEILieQKRQKLSTVEKLDEHmDFASQLIFAQ--NRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEK 330
Cdd:cd11060 182 ALEAV--AERLAEDAESAKGRK-DMLDSFLEAGlkDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAK 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   331 MMREIET---------VMGDREVQSddMPNLKIVenfIYESMRYQPVVDLIM-RKALQD-DVIDGYPVKKGTNIILNIGR 399
Cdd:cd11060 259 LRAEIDAavaegklssPITFAEAQK--LPYLQAV---IKEALRLHPPVGLPLeRVVPPGgATICGRFIPGGTIVGVNPWV 333
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117292   400 MHKLE--FFPKPNEF----SLENFEKNVP--SRYFQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKG 464
Cdd:cd11060 334 IHRDKevFGEDADVFrperWLEADEEQRRmmDRADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVDP 406
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
241-453 9.53e-19

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  Cd Length: 433  Bit Score: 88.42  E-value: 9.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   241 KKYEEAAKDLKGA-----MEILIEQKRqklstveklDEHMDFAsqlifaqnrgdLTAENVNQCVLEMMIAAPDTLSVTLF 315
Cdd:cd20655 190 KEHEEKRKKRKEGgskdlLDILLDAYE---------DENAEYK-----------ITRNHIKAFILDLFIAGTDTSAATTE 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   316 IMLILIADDPTVEEKMMREIETVMG-DREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNII 394
Cdd:cd20655 250 WAMAELINNPEVLEKAREEIDSVVGkTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKINGYDIPEKTTLF 329
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 117292   395 LN---IGRmhKLEFFPKPNEFSLENFEKNVPS--------RYFQ--PFGFGPRGCVGKFIAMVMMKAILVTL 453
Cdd:cd20655 330 VNvyaIMR--DPNYWEDPLEFKPERFLASSRSgqeldvrgQHFKllPFGSGRRGCPGASLAYQVVGTAIAAM 399
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
132-460 2.12e-18

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235  Cd Length: 502  Bit Score: 87.82  E-value: 2.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    132 IFNNNPAHWKEIRPFFTKALSGPGL----VRMIAICVESTIVHLdkLEEVTTEvGNVNVLNL---MRRIMLDTSNK---- 200
Cdd:PLN02426 123 IFNVDGDSWRFQRKMASLELGSVSIrsyaFEIVASEIESRLLPL--LSSAADD-GEGAVLDLqdvFRRFSFDNICKfsfg 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    201 -----LFLGVPLDESAIVLKIQNYFDAWQALLLKPdIFFKISWLC-----KKYEEAAKDLKGAMEILIEQKRqklstVEK 270
Cdd:PLN02426 200 ldpgcLELSLPISEFADAFDTASKLSAERAMAASP-LLWKIKRLLnigseRKLKEAIKLVDELAAEVIRQRR-----KLG 273
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    271 LDEHMDFASQliFAQNRGDltAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDREVQS--DD 348
Cdd:PLN02426 274 FSASKDLLSR--FMASIND--DKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAAsfEE 349
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    349 MPNLKIVENFIYESMRYQPVVDLIMRKALQDDVI-DGYPVKKGTNIILN---IGRMHK------LEFFP----KPNEFSL 414
Cdd:PLN02426 350 MKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLpDGTFVAKGTRVTYHpyaMGRMERiwgpdcLEFKPerwlKNGVFVP 429
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 117292    415 ENfeknvPSRY--FQPfgfGPRGCVGKFIAMVMMKAILVTLLRRCRVQ 460
Cdd:PLN02426 430 EN-----PFKYpvFQA---GLRVCLGKEMALMEMKSVAVAVVRRFDIE 469
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
225-456 3.88e-18

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: 86.51  E-value: 3.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   225 ALLLKPDIFFKISWLCKKYEEAAKDLKGAMEILIEQKRQKLSTveKLDEHMDFASQLIFAQN--------RGDLTAENVN 296
Cdd:cd11061 146 GVLGHAPWLRPLLLDLPLFPGATKARKRFLDFVRAQLKERLKA--EEEKRPDIFSYLLEAKDpetgegldLEELVGEARL 223
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   297 qcvleMMIAAPDTLSVTL-FIMLILiADDPTVEEKMMREIETVM--GDREVQSDDMPNLKIVENFIYESMR-YQPVVDLI 372
Cdd:cd11061 224 -----LIVAGSDTTATALsAIFYYL-ARNPEAYEKLRAELDSTFpsDDEIRLGPKLKSLPYLRACIDEALRlSPPVPSGL 297
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   373 MRKALQDDV-IDGYPVKKGTNI---ILNIGRMHKLefFPKPNEFslenfeknVPSR-------------YFQPFGFGPRG 435
Cdd:cd11061 298 PRETPPGGLtIDGEYIPGGTTVsvpIYSIHRDERY--FPDPFEF--------IPERwlsrpeelvrarsAFIPFSIGPRG 367
                       250       260
                ....*....|....*....|.
gi 117292   436 CVGKFIAMVMMKAILVTLLRR 456
Cdd:cd11061 368 CIGKNLAYMELRLVLARLLHR 388
PTZ00404 PTZ00404
cytochrome P450; Provisional
294-443 4.57e-18

cytochrome P450; Provisional


Pssm-ID: 173595  Cd Length: 482  Bit Score: 86.70  E-value: 4.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292    294 NVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDR-EVQSDDMPNLKIVENFIYESMRYQPVVDL- 371
Cdd:PTZ00404 283 SILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRnKVLLSDRQSTPYTVAIIKETLRYKPVSPFg 362
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 117292    372 IMRKALQDDVI-DGYPVKKGTNIILN---IGRMHKleFFPKPNEFSLENFEKNVPSRYFQPFGFGPRGCVGKFIAM 443
Cdd:PTZ00404 363 LPRSTSNDIIIgGGHFIPKDAQILINyysLGRNEK--YFENPEQFDPSRFLNPDSNDAFMPFSIGPRNCVGQQFAQ 436
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
128-446 7.88e-18

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: 85.38  E-value: 7.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   128 ENGIIFNNNPAHwKEIR----PFFT-KALsgpGLVRMIAicvESTIV-HLDKLEEVTTEVGN-VNVLNLMRRIMLDTSNK 200
Cdd:cd11082  47 EDNLIFMFGEEH-KELRksllPLFTrKAL---GLYLPIQ---ERVIRkHLAKWLENSKSGDKpIEMRPLIRDLNLETSQT 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   201 LFLGVPLDESAIVLKIqNYFDAWQALLLKPdIFFKISWLCKKYEeAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDFASQ 280
Cdd:cd11082 120 VFVGPYLDDEARRFRI-DYNYFNVGFLALP-VDFPGTALWKAIQ-ARKRIVKTLEKCAAKSKKRMAAGEEPTCLLDFWTH 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   281 LIFA----------QNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMREIETVMGDRE--VQSDD 348
Cdd:cd11082 197 EILEeikeaeeegePPPPHSSDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDEppLTLDL 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   349 MPNLKIVENFIYESMRYQPVVDLIMRKALQDDVI-DGYPVKKGTNIILNI-GRMHklEFFPKPNEFSLENF-----EKNV 421
Cdd:cd11082 277 LEEMKYTRQVVKEVLRYRPPAPMVPHIAKKDFPLtEDYTVPKGTIVIPSIyDSCF--QGFPEPDKFDPDRFsperqEDRK 354
                       330       340       350
                ....*....|....*....|....*....|....
gi 117292   422 PSRYFQPFGFGPRGCVGK---------FIAMVMM 446
Cdd:cd11082 355 YKKNFLVFGAGPHQCVGQeyainhlmlFLALFST 388
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
258-464 9.29e-18

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  Cd Length: 432  Bit Score: 85.25  E-value: 9.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   258 IEQK-RQKLSTVEKLDEHMDfASQLIFAQNRGD---LTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMR 333
Cdd:cd20638 191 IEENiRAKIQREDTEQQCKD-ALQLLIEHSRRNgepLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRK 269
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   334 EIET--VMG-----DREVQSDDMPNLKIVENFIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHKL-EF 405
Cdd:cd20638 270 ELQEkgLLStkpneNKELSMEVLEQLKYTGCVIKETLRLSPPVPGGFRVALKTFELNGYQIPKGWNVIYSICDTHDVaDI 349
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 117292   406 FPKPNEFSLENFEKNVP---SRY-FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQTMKG 464
Cdd:cd20638 350 FPNKDEFNPDRFMSPLPedsSRFsFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNG 412
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
244-456 6.60e-17

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: 81.96  E-value: 6.60e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   244 EEAAKDLKGAMEILIEQKRQKLSTvekldehmDFASQLIFAQNRG-DLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIA 322
Cdd:cd20629 149 EAAAAELYDYVLPLIAERRRAPGD--------DLISRLLRAEVEGeKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLL 220
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   323 DDPTVeekmmreIETVMGDREVqsddMPNLkivenfIYESMRYQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK 402
Cdd:cd20629 221 QHPEQ-------LERVRRDRSL----IPAA------IEEGLRWEPPVASVPRMALRDVELDGVTIPAGSLLDLSVGSANR 283
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 117292   403 LE-FFPKPNEFSLenFEKNVPSryfQPFGFGPRGCVGKFIAMVMMKAILVTLLRR 456
Cdd:cd20629 284 DEdVYPDPDVFDI--DRKPKPH---LVFGGGAHRCLGEHLARVELREALNALLDR 333
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
241-460 1.58e-16

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: 81.63  E-value: 1.58e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   241 KKYEEAAKDLKGAMEILIEQKRQKLStvEKLDEHMDFASQ-LIFAQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLI 319
Cdd:cd20646 181 KRYVDAWDTIFSFGKKLIDKKMEEIE--ERVDRGEPVEGEyLTYLLSSGKLSPKEVYGSLTELLLAGVDTTSNTLSWALY 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   320 LIADDPTVEEKMMREIETVM-GDREVQSDD---MPNLKIVenfIYESMRYQPVVDLIMRKALQDDVIDG-YPVKKGTNII 394
Cdd:cd20646 259 HLARDPEIQERLYQEVISVCpGDRIPTAEDiakMPLLKAV---IKETLRLYPVVPGNARVIVEKEVVVGdYLFPKNTLFH 335
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 117292   395 L-NIGRMHKLEFFPKPNEFSLENFEKNVPSRY----FQPFGFGPRGCVGKFIAMVMMKAILVTLLRRCRVQ 460
Cdd:cd20646 336 LcHYAVSHDETNFPEPERFKPERWLRDGGLKHhpfgSIPFGYGVRACVGRRIAELEMYLALSRLIKRFEVR 406
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
139-451 1.95e-16

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: 81.52  E-value: 1.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   139 HWKEIRPFFTKALSGPGLVRMIAICVESTI-VHLDKL-EEVTTEVGNVNVLNLMRRIMLDTSNKLFLGVPLDESAI---- 212
Cdd:cd11075  63 LWRTLRRNLVSEVLSPSRLKQFRPARRRALdNLVERLrEEAKENPGPVNVRDHFRHALFSLLLYMCFGERLDEETVrele 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   213 -----VLKIQNYFDaWQALL--LKPdIFFKISWlcKKYEEAAKDLKGAMEILIEQKRQKLSTVEKLDEHMDF----ASQL 281
Cdd:cd11075 143 rvqreLLLSFTDFD-VRDFFpaLTW-LLNRRRW--KKVLELRRRQEEVLLPLIRARRKRRASGEADKDYTDFllldLLDL 218
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   282 IFAQNRGDLT-AENVNQCVlEMMIAAPDTLSVTL-FIMLILIADdPTVEEKMMREIETVMGDREVQSDD----MPNLKIV 355
Cdd:cd11075 219 KEEGGERKLTdEELVSLCS-EFLNAGTDTTATALeWAMAELVKN-PEIQEKLYEEIKEVVGDEAVVTEEdlpkMPYLKAV 296
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   356 enfIYESMR-YQPVVDLIMRKALQDDVIDGYPVKKGTNIILNIGRMHK--------LEFfpKPNEFSLENFEKNVP--SR 424
Cdd:cd11075 297 ---VLETLRrHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRdpkvwedpEEF--KPERFLAGGEAADIDtgSK 371
                       330       340       350
                ....*....|....*....|....*....|..
gi 117292   425 YFQ--PFGFGPRGCVGKFIAMV---MMKAILV 451
Cdd:cd11075 372 EIKmmPFGAGRRICPGLGLATLhleLFVARLV 403
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
303-461 2.48e-16

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: 81.04  E-value: 2.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   303 MIAAPDTLSVTLFIMLILIADDPTVEEKMMREIEtVMGDREVQSD--DMPNLKIVENFIYESMRYQPVVDLIMRKALQDD 380
Cdd:cd20649 270 LIAGYETTTNTLSFATYLLATHPECQKKLLREVD-EFFSKHEMVDyaNVQELPYLDMVIAETLRMYPPAFRFAREAAEDC 348
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   381 VIDGYPVKKGTNIILNIGRMH-KLEFFPKPNEFSLENFEKNVPSRY----FQPFGFGPRGCVGKFIAMVMMKAILVTLLR 455
Cdd:cd20649 349 VVLGQRIPAGAVLEIPVGFLHhDPEHWPEPEKFIPERFTAEAKQRRhpfvYLPFGAGPRSCIGMRLALLEIKVTLLHILR 428

                ....*.
gi 117292   456 RCRVQT 461
Cdd:cd20649 429 RFRFQA 434
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
258-454 2.48e-16

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


Pssm-ID: 410751  Cd Length: 444  Bit Score: 81.26  E-value: 2.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   258 IEQKRQKLSTVEKldehmDFASQLIF---AQNRGDLTAENVNQCVLEMMIAAPDTLSVTLFIMLILIADDPTVEEKMMRE 334
Cdd:cd20658 203 IKQWREGKKKEEE-----DWLDVFITlkdENGNPLLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEE 277
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 117292   335 IETVMG-DREVQSDDMPNLKIVENFIYESMRYQPVVDLIM-RKALQDDVIDGYPVKKGTNIILN---IGRMHKleFFPKP 409
Cdd:cd20658 278 LDRVVGkERLVQESDIPNLNYVKACAREAFRLHPVAPFNVpHVAMSDTTVGGYFIPKGSHVLLSrygLGRNPK--VWDDP 355
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 117292   410 NEFSLE---NFEKNV----PSRYFQPFGFGPRGCVGKFIAMVMMKAILVTLL 454
Cdd:cd20658 356 LKFKPErhlNEDSEVtltePDLRFISFSTGRRGCPGVKLGTAMTVMLLARLL 407
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
286-459 6.15e-16

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