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Conserved domains on  [gi|13449277|ref|NP_085125|]
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cytochrome P450 2S1 precursor [Homo sapiens]

Protein Classification

cytochrome P450( domain architecture ID 15296224)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
64-490 0e+00

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


:

Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 710.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd11026   1 YGPVFTVYLG-SKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd11026  80 SIEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd11026 160 PPLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSP-RDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd11026 239 TETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd11026 319 YTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSL 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd11026 399 SSPVGPKDPDLTPRFSGFTNSPRPYQL 425
 
Name Accession Description Interval E-value
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
64-490 0e+00

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 710.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd11026   1 YGPVFTVYLG-SKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd11026  80 SIEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd11026 160 PPLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSP-RDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd11026 239 TETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd11026 319 YTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSL 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd11026 399 SSPVGPKDPDLTPRFSGFTNSPRPYQL 425
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
49-492 3.29e-140

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: 411.67  E-value: 3.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277    49 RPGALYSGLMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLE---GTFDGHGVFFSNGERWR 125
Cdd:pfam00067  18 RKGNLHSVFTKLQKKYGPIFRLYLGP-KPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFAtsrGPFLGKGIVFANGPRWR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   126 QLRKFTMLALRdlGMGKREGEELIQAEARCLVETFQGTEGRP--FDPSLLLAQATSNVVCSLLFGLRF-SYEDKEFQAVV 202
Cdd:pfam00067  97 QLRRFLTPTFT--SFGKLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFgSLEDPKFLELV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   203 RAAGGTLLGVSSQGGQTYEMFSWfLRPLPGPHKQLLHHV-STLAAFTVRQVQQHQGNLD-ASGPARDLVDAFLLKMAQEE 280
Cdd:pfam00067 175 KAVQELSSLLSSPSPQLLDLFPI-LKYFPGPHGRKLKRArKKIKDLLDKLIEERRETLDsAKKSPRDFLDALLLAKEEED 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   281 qnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA 360
Cdd:pfam00067 254 ---GSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKET 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   361 QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVC 440
Cdd:pfam00067 331 LRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNC 410
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13449277   441 LGEGLAKAELFLFFTTILQAFSLEsPCPPDTLSLKPTVSGLFNIPPAFQLQV 492
Cdd:pfam00067 411 LGERLARMEMKLFLATLLQNFEVE-LPPGTDPPDIDETPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
49-477 2.03e-44

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 161.44  E-value: 2.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  49 RPGALYSGLMRLSKKYGPVFTIYL-GPWRPVVVLVGQEAVREALGgQAEEFSGRGTVAM----LEGTFDGHGVFFSNGER 123
Cdd:COG2124  20 LEFAPRFFLERAEDPYGDYFTLRLpGPGDGFWVVSRPADVREVLR-DPRFFSSALGAGLrprlLRPVLGDGSLLTLDGPE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 124 WRQLRKFTMLALRdlGMGKREGEELIQAEARCLVETFQGteGRPFDPSLLLAQATSNVVCSLlFGLRFSYEDKEFQAVVR 203
Cdd:COG2124  99 HTRLRKLLAPAFT--PRALRGYRPLIREIADRLLDDLWQ--GGADLVLDFAAELTLRVIAEL-LGVPLEDRPQLLRWSDA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 204 AAggtllgvssqggqtyeMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNldasgPARDLVDAfllkMAQEEQNP 283
Cdd:COG2124 174 LL----------------LRLDPDLGPEEPWRRARAARRELDAYLRALIAERRAA-----PRDDLLSL----LLSAEDDG 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 284 GTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRelgagqapslgdrtrlPYTDAVLHEAQRL 363
Cdd:COG2124 229 GGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR----------------PLLEAVVEETLRL 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 364 LALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFldadgrfrkHEAFLPFSLGKRVCLGE 443
Cdd:COG2124 293 YPPVPL-ARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERF---------NNAHLPFGGGPHRCLGA 362
                       410       420       430
                ....*....|....*....|....*....|....
gi 13449277 444 GLAKAELFLFFTTILQAFSLESPCPPDTLSLKPT 477
Cdd:COG2124 363 ALARLELKVALAELLRRFPLLLLAEPPPLVRRPT 396
PTZ00404 PTZ00404
cytochrome P450; Provisional
54-465 2.76e-41

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 154.11  E-value: 2.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   54 YSGLMRLSKKYGPVFTIYLGPWRpVVVLVGQEAVREALGGQAEEFSGRGTVAMLE-GTFdGHGVFFSNGERWRQLRKFTM 132
Cdd:PTZ00404  51 HRDLTKMSKKYGGIFRIWFADLY-TVVLSDPILIREMFVDNFDNFSDRPKIPSIKhGTF-YHGIVTSSGEYWKRNREIVG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  133 LALRDLGMgkREGEELIQAEARCLVETFQGTE--GRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKefqaVVRAAGGTLL 210
Cdd:PTZ00404 129 KAMRKTNL--KHIYDLLDDQVDVLIESMKKIEssGETFEPRYYLTKFTMSAMFKYIFNEDISFDED----IHNGKLAELM 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  211 GVSSQGGQTYEMFSWF-----LRPLPgpHKQLLH---HVSTLAAFTVRQVQQHQGNLDASGPaRDLVDaFLLKmaqeEQN 282
Cdd:PTZ00404 203 GPMEQVFKDLGSGSLFdvieiTQPLY--YQYLEHtdkNFKKIKKFIKEKYHEHLKTIDPEVP-RDLLD-LLIK----EYG 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  283 PGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:PTZ00404 275 TNTDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLR 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  363 LLALVPMGIPRTLMR-TTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADgrfrKHEAFLPFSLGKRVCL 441
Cdd:PTZ00404 355 YKPVSPFGLPRSTSNdIIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SNDAFMPFSIGPRNCV 430
                        410       420
                 ....*....|....*....|....
gi 13449277  442 GEGLAKAELFLFFTTILQAFSLES 465
Cdd:PTZ00404 431 GQQFAQDELYLAFSNIILNFKLKS 454
 
Name Accession Description Interval E-value
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
64-490 0e+00

cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, most diverse CYP families in vertebrates. It includes many subfamilies across vertebrate species but not all subfamilies are found in multiple vertebrate taxonomic classes. The CYP2U and CYP2R genes are present in the vertebrate ancestor and are shared across all vertebrate classes, whereas some subfamilies are lineage-specific, such as CYP2B and CYP2S in mammals. CYP2 enzymes play important roles in drug metabolism. The CYP2 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410652 [Multi-domain]  Cd Length: 425  Bit Score: 710.87  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd11026   1 YGPVFTVYLG-SKPVVVLCGYEAVKEALVDQAEEFSGRPPVPLFDRVTKGYGVVFSNGERWKQLRRFSLTTLRNFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd11026  80 SIEERIQEEAKFLVEAFRKTKGKPFDPTFLLSNAVSNVICSIVFGSRFDYEDKEFLKLLDLINENLRLLSSPWGQLYNMF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd11026 160 PPLLKHLPGPHQKLFRNVEEIKSFIRELVEEHRETLDPSSP-RDFIDCFLLKMEKEKDNPNSEFHEENLVMTVLDLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd11026 239 TETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLEDRAKMPYTDAVIHEVQRFGDIVPLGVPHAVTRDTKFRG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd11026 319 YTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFLDEQGKFKKNEAFMPFSAGKRVCLGEGLARMELFLFFTSLLQRFSL 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd11026 399 SSPVGPKDPDLTPRFSGFTNSPRPYQL 425
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
64-490 0e+00

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


Pssm-ID: 410763 [Multi-domain]  Cd Length: 425  Bit Score: 535.27  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20670   1 YGPVFTVYMGP-RPVVVLCGHEAVKEALVDQADEFSGRGELATIERNFQGHGVALANGERWRILRRFSLTILRNFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20670  80 SIEERIQEEAGYLLEEFRKTKGAPIDPTFFLSRTVSNVISSVVFGSRFDYEDKQFLSLLRMINESFIEMSTPWAQLYDMY 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20670 160 SGIMQYLPGRHNRIYYLIEELKDFIASRVKINEASLDPQNP-RDFIDCFLIKMHQDKNNPHTEFNLKNLVLTTLNLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20670 239 TETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVDDRVKMPYTDAVIHEIQRLTDIVPLGVPHNVIRDTQFRG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20670 319 YLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFLDEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSL 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20670 399 RSLVPPADIDITPKISGFGNIPPTYEL 425
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
64-490 0e+00

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


Pssm-ID: 410758 [Multi-domain]  Cd Length: 425  Bit Score: 532.61  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20665   1 YGPVFTLYLGM-KPTVVLHGYEAVKEALIDLGEEFSGRGRFPIFEKVNKGLGIVFSNGERWKETRRFSLMTLRNFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20665  80 SIEDRVQEEARCLVEELRKTNGSPCDPTFILGCAPCNVICSIIFQNRFDYKDQDFLNLMEKLNENFKILSSPWLQVCNNF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20665 160 PALLDYLPGSHNKLLKNVAYIKSYILEKVKEHQESLDVNNP-RDFIDCFLIKMEQEKHNQQSEFTLENLAVTVTDLFGAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20665 239 TETTSTTLRYGLLLLLKHPEVTAKVQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPNNLPHAVTCDTKFRN 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20665 319 YLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFLDENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNL 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20665 399 KSLVDPKDIDTTPVVNGFASVPPPYQL 425
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
64-490 0e+00

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


Pssm-ID: 410765 [Multi-domain]  Cd Length: 425  Bit Score: 521.65  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20672   1 YGDVFTVHLGP-RPVVMLCGTDAIREALVDQAEAFSGRGTIAVVDPIFQGYGVIFANGERWKTLRRFSLATMRDFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20672  80 SVEERIQEEAQCLVEELRKSKGALLDPTFLFQSITANIICSIVFGERFDYKDPQFLRLLDLFYQTFSLISSFSSQVFELF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20672 160 SGFLKYFPGAHRQIYKNLQEILDYIGHSVEKHRATLDPSAP-RDFIDTYLLRMEKEKSNHHTEFHHQNLMISVLSLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20672 239 TETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDDRAKMPYTDAVIHEIQRFSDLIPIGVPHRVTKDTLFRG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20672 319 YLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFLDANGALKKSEAFMPFSTGKRICLGEGIARNELFLFFTTILQNFSV 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20672 399 ASPVAPEDIDLTPKESGVGKIPPTYQI 425
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
64-490 4.90e-180

cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes CYP2A1, 2A2, and 2A3 in rats; CYP2A4, 2A5, 2A12, 2A20p, 2A21p, 2A22, and 2A23p in mice; CYP2A6, 2A7, 2A13, 2A18P in humans; CYP2A8, 2A9, 2A14, 2A15, 2A16, and 2A17 in hamsters; CYP2A10 and 2A11 in rabbits; and CYP2A19 in pigs. CYP2A enzymes metabolize numerous xenobiotic compounds, including coumarin, aflatoxin B1, nicotine, cotinine, 1,3-butadiene, and acetaminophen, among others, as well as endogenous compounds, including testosterone, progesterone, and other steroid hormones. Human CYP2A6 is responsible for the systemic clearance of nicotine, while CYP2A13 activates the nicotine-derived procarcinogen 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone (NNK) into DNA-altering compounds that cause lung cancer. The CYP2A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410761 [Multi-domain]  Cd Length: 425  Bit Score: 511.65  E-value: 4.90e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20668   1 YGPVFTIHLGP-RRVVVLCGYDAVKEALVDQAEEFSGRGEQATFDWLFKGYGVAFSNGERAKQLRRFSIATLRDFGVGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20668  80 GIEERIQEEAGFLIDALRGTGGAPIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSFQFTATSTGQLYEMF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20668 160 SSVMKHLPGPQQQAFKELQGLEDFIAKKVEHNQRTLDPNSP-RDFIDSFLIRMQEEKKNPNTEFYMKNLVMTTLNLFFAG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20668 239 TETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFEDRAKMPYTEAVIHEIQRFGDVIPMGLARRVTKDTKFRD 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20668 319 FFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTIMQNFRF 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20668 399 KSPQSPEDIDVSPKHVGFATIPRNYTM 425
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
64-490 1.27e-178

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


Pssm-ID: 410762 [Multi-domain]  Cd Length: 425  Bit Score: 508.15  E-value: 1.27e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20669   1 YGSVYTVYLGP-RPVVVLCGYQAVKEALVDQAEEFSGRGDYPVFFNFTKGNGIAFSNGERWKILRRFALQTLRNFGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20669  80 SIEERILEEAQFLLEELRKTKGAPFDPTFLLSRAVSNIICSVVFGSRFDYDDKRLLTILNLINDNFQIMSSPWGELYNIF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20669 160 PSVMDWLPGPHQRIFQNFEKLRDFIAESVREHQESLDPNSP-RDFIDCFLTKMAEEKQDPLSHFNMETLVMTTHNLLFGG 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20669 239 TETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLEDRARMPYTDAVIHEIQRFADIIPMSLPHAVTRDTNFRG 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20669 319 FLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFLDDNGSFKKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSL 398
                       410       420
                ....*....|....*....|....*..
gi 13449277 464 ESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20669 399 QPLGAPEDIDLTPLSSGLGNVPRPFQL 425
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
64-486 3.82e-150

cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and amphibians. CYP2K6 from zebrafish has been shown to catalyze the conversion of aflatoxin B1 (AFB1) to its cytotoxic derivative AFB1 exo-8,9-epoxide, while its ortholog in rainbow trout CYP2K1 is also capable of oxidizing lauric acid. In birds, CYP2K is one of the largest CYP2 subfamilies. The CYP2K subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410757 [Multi-domain]  Cd Length: 424  Bit Score: 435.77  E-value: 3.82e-150
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20664   1 YGSIFTVQMGT-KKVVVLAGYKTVKEALVNHAEAFGGRPIIPIFEDFNKGYGILFSNGENWKEMRRFTLTTLRDFGMGKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20664  80 TSEDKILEEIPYLIEVFEKHKGKPFETTLSMNVAVSNIIASIVLGHRFEYTDPTLLRMVDRINENMKLTGSPSVQLYNMF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWfLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20664 160 PW-LGPFPGDINKLLRNTKELNDFLMETFMKHLDVLEPNDQ-RGFIDAFLVKQQEEEESSDSFFHDDNLTCSVGNLFGAG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQaPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20664 238 TDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIGSRQ-PQVEHRKNMPYTDAVIHEIQRFANIVPMNLPHATTRDVTFRG 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20664 317 YFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFLDSQGKFVKRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRF 396
                       410       420
                ....*....|....*....|....*
gi 13449277 464 ESPCPP--DTLSLKPTVSglFNIPP 486
Cdd:cd20664 397 QPPPGVseDDLDLTPGLG--FTLNP 419
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
49-492 3.29e-140

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: 411.67  E-value: 3.29e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277    49 RPGALYSGLMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLE---GTFDGHGVFFSNGERWR 125
Cdd:pfam00067  18 RKGNLHSVFTKLQKKYGPIFRLYLGP-KPVVVLSGPEAVKEVLIKKGEEFSGRPDEPWFAtsrGPFLGKGIVFANGPRWR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   126 QLRKFTMLALRdlGMGKREGEELIQAEARCLVETFQGTEGRP--FDPSLLLAQATSNVVCSLLFGLRF-SYEDKEFQAVV 202
Cdd:pfam00067  97 QLRRFLTPTFT--SFGKLSFEPRVEEEARDLVEKLRKTAGEPgvIDITDLLFRAALNVICSILFGERFgSLEDPKFLELV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   203 RAAGGTLLGVSSQGGQTYEMFSWfLRPLPGPHKQLLHHV-STLAAFTVRQVQQHQGNLD-ASGPARDLVDAFLLKMAQEE 280
Cdd:pfam00067 175 KAVQELSSLLSSPSPQLLDLFPI-LKYFPGPHGRKLKRArKKIKDLLDKLIEERRETLDsAKKSPRDFLDALLLAKEEED 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   281 qnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEA 360
Cdd:pfam00067 254 ---GSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKET 330
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   361 QRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVC 440
Cdd:pfam00067 331 LRLHPVVPLLLPREVTKDTVIPGYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDENGKFRKSFAFLPFGAGPRNC 410
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 13449277   441 LGEGLAKAELFLFFTTILQAFSLEsPCPPDTLSLKPTVSGLFNIPPAFQLQV 492
Cdd:pfam00067 411 LGERLARMEMKLFLATLLQNFEVE-LPPGTDPPDIDETPGLLLPPKPYKLKF 461
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
64-487 2.25e-131

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


Pssm-ID: 410755 [Multi-domain]  Cd Length: 421  Bit Score: 387.62  E-value: 2.25e-131
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20662   1 YGNIFSLQLGS-ISSVIVTGLPLIKEALVTQEQNFMNRPETPLRERIFNKNGLIFSSGQTWKEQRRFALMTLRNFGLGKK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20662  80 SLEERIQEECRHLVEAIREEKGNPFNPHFKINNAVSNIICSVTFGERFEYHDEWFQELLRLLDETVYLEGSPMSQLYNAF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQeEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20662 160 PWIMKYLPGSHQTVFSNWKKLKLFVSDMIDKHREDWNPDEP-RDFIDAYLKEMAK-YPDPTTSFNEENLICSTLDLFFAG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20662 238 TETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADRESMPYTNAVIHEVQRMGNIIPLNVPREVAVDTKLAG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDaDGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20662 318 FHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFLE-NGQFKKREAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTF 396
                       410       420
                ....*....|....*....|....
gi 13449277 464 eSPCPPDTLSLKPTVSglFNIPPA 487
Cdd:cd20662 397 -KPPPNEKLSLKFRMG--ITLSPV 417
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
64-466 3.69e-127

cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The function of CYP2AB1 is unknown. CYP2AB1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 376.87  E-value: 3.69e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20667   1 YGNIYTLWLGS-TPIVVLSGFKAVKEGLVSHSEEFSGRPLTPFFRDLFGEKGIICTNGLTWKQQRRFCMTTLRELGLGKQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20667  80 ALESQIQHEAAELVKVFAQENGRPFDPQDPIVHATANVIGAVVFGHRFSSEDPIFLELIRAINLGLAFASTIWGRLYDAF 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNlDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20667 160 PWLMRYLPGPHQKIFAYHDAVRSFIKKEVIRHELR-TNEAP-QDFIDCYLAQITKTKDDPVSTFSEENMIQVVIDLFLGG 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRG 383
Cdd:cd20667 238 TETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQLICYEDRKRLPYTNAVIHEVQRLSNVVSVGAVRQCVTSTTMHG 317
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20667 318 YYVEKGTIILPNLASVLYDPECWETPHKFNPGHFLDKDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIFFTTLLRTFNF 397

                ...
gi 13449277 464 ESP 466
Cdd:cd20667 398 QLP 400
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
64-490 1.87e-124

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


Pssm-ID: 410756 [Multi-domain]  Cd Length: 428  Bit Score: 370.18  E-value: 1.87e-124
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGH---GVFFSN-GERWRQLRKFTMLALRDLG 139
Cdd:cd20663   1 FGDVFSLQMA-WKPVVVLNGLKAVREALVTCGEDTADRPPVPIFEHLGFGPksqGVVLARyGPAWREQRRFSVSTLRNFG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 140 MGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQT 219
Cdd:cd20663  80 LGKKSLEQWVTEEAGHLCAAFTDQAGRPFNPNTLLNKAVCNVIASLIFARRFEYEDPRFIRLLKLLEESLKEESGFLPEV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 220 YEMFSWFLRpLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYL 299
Cdd:cd20663 160 LNAFPVLLR-IPGLAGKVFPGQKAFLALLDELLTEHRTTWDPAQPPRDLTDAFLAEMEKAKGNPESSFNDENLRLVVADL 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 300 LFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTT 379
Cdd:cd20663 239 FSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMADQARMPYTNAVIHEVQRFGDIVPLGVPHMTSRDI 318
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 380 RFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQ 459
Cdd:cd20663 319 EVQGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFLDAQGHFVKPEAFMPFSAGRRACLGEPLARMELFLFFTCLLQ 398
                       410       420       430
                ....*....|....*....|....*....|....*
gi 13449277 460 AFSLE----SPCPPDTlslkpTVSGLFNIPPAFQL 490
Cdd:cd20663 399 RFSFSvpagQPRPSDH-----GVFAFLVSPSPYQL 428
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
65-490 1.00e-118

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: 355.37  E-value: 1.00e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALggQAEEFSGRGTVAMLE-GTFDGH-GVFFSNGERWRQLRKFTMLALRDLGMGK 142
Cdd:cd20651   1 GDVVGLKLGK-DKVVVVSGYEAVREVL--SREEFDGRPDGFFFRlRTFGKRlGITFTDGPFWKEQRRFVLRHLRDFGFGR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKE----------FQAVVRAAGGTLlgv 212
Cdd:cd20651  78 RSMEEVIQEEAEELIDLLKKGEKGPIQMPDLFNVSVLNVLWAMVAGERYSLEDQKlrkllelvhlLFRNFDMSGGLL--- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 213 sSQggqtyemFSW--FLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMaQEEQNPGTEFTNK 290
Cdd:cd20651 155 -NQ-------FPWlrFIAPEFSGYNLLVELNQKLIEFLKEEIKEHKKTYDEDNP-RDLIDAYLREM-KKKEPPSSSFTDD 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 291 NMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMG 370
Cdd:cd20651 225 QLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIG 304
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 371 IPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAEL 450
Cdd:cd20651 305 IPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFLDEDGKLLKDEWFLPFGAGKRRCLGESLARNEL 384
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 13449277 451 FLFFTTILQAFSLESPCPPDTlSLKPTVSGLFNIPPAFQL 490
Cdd:cd20651 385 FLFFTGLLQNFTFSPPNGSLP-DLEGIPGGITLSPKPFRV 423
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
64-490 5.17e-118

cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is expressed during development of the gastrointestinal tract, is silenced after birth in the intestine and colon by epigenetic modifications, but is activated following demethylation in colorectal cancer (CRC). Its expression levels in CRC correlate with the degree of malignancy, are higher in metastases and are predictive of survival. Thus, it is an attractive tumor-specific diagnostic and therapeutic target. CYP2W1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410764 [Multi-domain]  Cd Length: 422  Bit Score: 353.33  E-value: 5.17e-118
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd20671   1 YGPVFTIHLGM-QKTVVLTGYEAVKEALVGTGDEFADRPPIPIFQAIQHGNGVFFSSGERWRTTRRFTVRSMKSLGMGKR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EGEELIQAEARCLVETFQGTEGRPFdPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTYEMF 223
Cdd:cd20671  80 TIEDKILEELQFLNGQIDSFNGKPF-PLRLLGWAPTNITFAMLFGRRFDYKDPTFVSLLDLIDEVMVLLGSPGLQLFNLY 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWfLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDaSGPARDLVDAFLLKmaQEEQNPG-TEFTNKNMLMTVIYLLFA 302
Cdd:cd20671 159 PV-LGAFLKLHKPILDKVEEVCMILRTLIEARRPTID-GNPLHSYIEALIQK--QEEDDPKeTLFHDANVLACTLDLVMA 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 303 GTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFR 382
Cdd:cd20671 235 GTETTSTTLQWAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPH-VPRCTAADTQFK 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 383 GYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFS 462
Cdd:cd20671 314 GYLIPKGTPVIPLLSSVLLDKTQWETPYQFNPNHFLDAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFT 393
                       410       420
                ....*....|....*....|....*...
gi 13449277 463 LESPCPPDTLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20671 394 FLPPPGVSPADLDATPAAAFTMRPQPQL 421
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
64-484 2.66e-116

cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific cytochrome P450 that catalyzes omega- and (omega-1)-hydroxylation of fatty acids such as arachidonic acid, docosahexaenoic acid, and other long chain fatty acids. Mutations in CYP2U1 are associated with hereditary spastic paraplegia (HSP), a neurological disorder, and pigmentary degenerative maculopathy associated with progressive spastic paraplegia. CYP2U1 belongs to family 2 of the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410759 [Multi-domain]  Cd Length: 426  Bit Score: 349.08  E-value: 2.66e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLALRDLGMGK 142
Cdd:cd20666   1 YGNIFSLFIGS-QLVVVLNDFESVREALVQKAEVFSDRPSVPLVTILTKGKGIVFAPyGPVWRQQRKFSHSTLRHFGLGK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQavvraaggTLLGVSSQG---GQT 219
Cdd:cd20666  80 LSLEPKIIEEFRYVKAEMLKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDYQDVEFK--------TMLGLMSRGleiSVN 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 220 YEMFSWFLRP----LP-GPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLM 294
Cdd:cd20666 152 SAAILVNICPwlyyLPfGPFRELRQIEKDITAFLKKIIADHRETLDPANP-RDFIDMYLLHIEEEQKNNAESSFNEDYLF 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 295 TVIY-LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPR 373
Cdd:cd20666 231 YIIGdLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPH 310
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 374 TLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd20666 311 MASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQLIKKEAFIPFGIGRRVCMGEQLAKMELFLM 390
                       410       420       430
                ....*....|....*....|....*....|.
gi 13449277 454 FTTILQAFSLESpcPPDTlsLKPTVSGLFNI 484
Cdd:cd20666 391 FVSLMQSFTFLL--PPNA--PKPSMEGRFGL 417
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
64-472 1.09e-115

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: 347.66  E-value: 1.09e-115
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGR-GTVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLALRDLGMG 141
Cdd:cd11027   1 YGDVFSLYLGS-RLVVVLNSGAAIKEALVKKSADFAGRpKLFTFDLFSRGGKDIAFGDySPTWKLHRKLAHSALRLYASG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 KREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGT--LLGVSSQggqt 219
Cdd:cd11027  80 GPRLEEKIAEEAEKLLKRLASQEGQPFDPKDELFLAVLNVICSITFGKRYKLDDPEFLRLLDLNDKFfeLLGAGSL---- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 220 YEMFSWfLRPLPGPH-KQLLHHVSTLAAFTVRQVQQHQGNLDaSGPARDLVDAfLLKMAQEEQNPGTE----FTNKNMLM 294
Cdd:cd11027 156 LDIFPF-LKYFPNKAlRELKELMKERDEILRKKLEEHKETFD-PGNIRDLTDA-LIKAKKEAEDEGDEdsglLTDDHLVM 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 295 TVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRT 374
Cdd:cd11027 233 TISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPTLSDRKRLPYLEATIAEVLRLSSVVPLALPHK 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 375 LMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKH-EAFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd11027 313 TTCDTTLRGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENGKLVPKpESFLPFSAGRRVCLGESLAKAELFLF 392
                       410       420
                ....*....|....*....|.
gi 13449277 454 FTTILQAFSLESP--CPPDTL 472
Cdd:cd11027 393 LARLLQKFRFSPPegEPPPEL 413
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
65-490 4.64e-113

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: 340.73  E-value: 4.64e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKRE 144
Cdd:cd20617   1 GGIFTLWLGD-VPTVVLSDPEIIKEAFVKNGDNFSDRPLLPSFEIISGGKGILFSNGDYWKELRRFALSSLTKTKLKKKM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 145 gEELIQAEARCLVETFQGTE--GRPFDPSLLLAQATSNVVCSLLFGLRFS-YEDKEFQAVVRAAGGtLLGVSSQGGQTYe 221
Cdd:cd20617  80 -EELIEEEVNKLIESLKKHSksGEPFDPRPYFKKFVLNIINQFLFGKRFPdEDDGEFLKLVKPIEE-IFKELGSGNPSD- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 222 mFSWFLRPLP-GPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPgtEFTNKNMLMTVIYLL 300
Cdd:cd20617 157 -FIPILLPFYfLYLKKLKKSYDKIKDFIEKIIEEHLKTIDPNNP-RDLIDDELLLLLKEGDSG--LFDDDSIISTCLDLF 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 301 FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTR 380
Cdd:cd20617 233 LAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPLGLPRVTTEDTE 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 381 FRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRfRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQA 460
Cdd:cd20617 313 IGGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFLENDGN-KLSEQFIPFGIGKRNCVGENLARDELFLFFANLLLN 391
                       410       420       430
                ....*....|....*....|....*....|
gi 13449277 461 FSLESPCPPdtLSLKPTVSGLFNIPPAFQL 490
Cdd:cd20617 392 FKFKSSDGL--PIDEKEVFGLTLKPKPFKV 419
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
64-498 2.05e-97

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


Pssm-ID: 410654 [Multi-domain]  Cd Length: 430  Bit Score: 300.75  E-value: 2.05e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFS-NGERWRQLRKFTMLALRDLGMGK 142
Cdd:cd11028   1 YGDVFQIRMGS-RPVVVLNGLETIKQALVRQGEDFAGRPDFYSFQFISNGKSMAFSdYGPRWKLHRKLAQNALRTFSNAR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REG--EELIQAEARCLVETFQGTEGR--PFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSqgGQ 218
Cdd:cd11028  80 THNplEEHVTEEAEELVTELTENNGKpgPFDPRNEIYLSVGNVICAICFGKRYSRDDPEFLELVKSNDDFGAFVGA--GN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 219 TYEMFSWfLRPLPGP----HKQLLHhvsTLAAFTVRQVQQHQGNLDaSGPARDLVDAfLLKMAQE---EQNPGTEFTNKN 291
Cdd:cd11028 158 PVDVMPW-LRYLTRRklqkFKELLN---RLNSFILKKVKEHLDTYD-KGHIRDITDA-LIKASEEkpeEEKPEVGLTDEH 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 292 MLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGI 371
Cdd:cd11028 232 IISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVPFTI 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 372 PRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRF--RKHEAFLPFSLGKRVCLGEGLAKAE 449
Cdd:cd11028 312 PHATTRDTTLNGYFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFLDDNGLLdkTKVDKFLPFGAGRRRCLGEELARME 391
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 13449277 450 LFLFFTTILQAFSLeSPCPPDTLSLKPTvsglfnippaFQLQVRPTDLH 498
Cdd:cd11028 392 LFLFFATLLQQCEF-SVKPGEKLDLTPI----------YGLTMKPKPFK 429
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
59-466 1.45e-87

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


Pssm-ID: 410754 [Multi-domain]  Cd Length: 436  Bit Score: 275.54  E-value: 1.45e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  59 RLSKKYGPVFTIYLGPWrPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLALRD 137
Cdd:cd20661   7 KQSQIHGQIFSLDLGGI-STVVLNGYDAVKECLVHQSEIFADRPSLPLFMKLTNMGGLLNSKyGRGWTEHRKLAVNCFRY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 138 LGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGG 217
Cdd:cd20661  86 FGYGQKSFESKISEECKFFLDAIDTYKGKPFDPKHLITNAVSNITNLIIFGERFTYEDTDFQHMIEIFSENVELAASAWV 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 218 QTYEMFSWfLRPLP-GPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPaRDLVDAFLLKMAQEEQNPGTEFTNKNMLMTV 296
Cdd:cd20661 166 FLYNAFPW-IGILPfGKHQQLFRNAAEVYDFLLRLIERFSENRKPQSP-RHFIDAYLDEMDQNKNDPESTFSMENLIFSV 243
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 297 IYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLM 376
Cdd:cd20661 244 GELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPLGIFHATS 323
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 377 RTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTT 456
Cdd:cd20661 324 KDAVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQFAKKEAFVPFSLGRRHCLGEQLARMEMFLFFTA 403
                       410
                ....*....|
gi 13449277 457 ILQAFSLESP 466
Cdd:cd20661 404 LLQRFHLHFP 413
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
64-494 6.11e-81

cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or Cyp17a1), also called cytochrome P450c17, steroid 17-alpha-hydroxylase (EC 1.14.14.19)/17,20 lyase (EC 1.14.14.32), or 17-alpha-hydroxyprogesterone aldolase, catalyzes the conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. It is a dual enzyme that catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reactions. Severe mutations on the enzyme cause combined 17-hydroxylase/17,20-lyase deficiency (17OHD); patients with 17OHD synthesize 11-deoxycorticosterone (DOC) which causes hypertension and hypokalemia. Loss of 17,20-lyase activity precludes sex steroid synthesis and leads to sexual infantilism. Included in this group is a second 17A P450 from teleost fish, CYP17A2, that is more efficient in pregnenolone 17-alpha-hydroxylation than CYP17A1, but does not catalyze the lyase reaction. CYP17A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410766 [Multi-domain]  Cd Length: 432  Bit Score: 258.40  E-value: 6.11e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPWRPVVVLVGQEAvREALGGQAEEFSGRG---TVAMLegTFDGHGVFFSN-GERWRQLRKFTMLALRDLG 139
Cdd:cd20673   1 YGPIYSLRMGSHTTVIVGHHQLA-KEVLLKKGKEFSGRPrmvTTDLL--SRNGKDIAFADySATWQLHRKLVHSAFALFG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 140 MGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSqgGQT 219
Cdd:cd20673  78 EGSQKLEKIICQEASSLCDTLATHNGESIDLSPPLFRAVTNVICLLCFNSSYKNGDPELETILNYNEGIVDTVAK--DSL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 220 YEMFSWfLRPLPGPH-KQLLHHVSTLAAFTVRQVQQHQGNLDaSGPARDLVDAFL-LKMAQEEQNPGT-----EFTNKNM 292
Cdd:cd20673 156 VDIFPW-LQIFPNKDlEKLKQCVKIRDKLLQKKLEEHKEKFS-SDSIRDLLDALLqAKMNAENNNAGPdqdsvGLSDDHI 233
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 293 LMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIP 372
Cdd:cd20673 234 LMTVGDIFGAGVETTTTVLKWIIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAPLLIP 313
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 373 RTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGrfrKH-----EAFLPFSLGKRVCLGEGLAK 447
Cdd:cd20673 314 HVALQDSSIGEFTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFLDPTG---SQlispsLSYLPFGAGPRVCLGEALAR 390
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 13449277 448 AELFLFFTTILQAFSLEspCPPDTlSLkPTVSGLFNIppafQLQVRP 494
Cdd:cd20673 391 QELFLFMAWLLQRFDLE--VPDGG-QL-PSLEGKFGV----VLQIDP 429
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
65-490 4.85e-80

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


Pssm-ID: 410745 [Multi-domain]  Cd Length: 432  Bit Score: 256.18  E-value: 4.85e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALggQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKRE 144
Cdd:cd20652   1 GSIFSLKMGS-VYTVVLSDPKLIRDTF--RRDEFTGRAPLYLTHGIMGGNGIICAEGDLWRDQRRFVHDWLRQFGMTKFG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 145 G-----EELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVR--AAGGTLLGVSSQGG 217
Cdd:cd20652  78 NgrakmEKRIATGVHELIKHLKAESGQPVDPSPVLMHSLGNVINDLVFGFRYKEDDPTWRWLRFlqEEGTKLIGVAGPVN 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 218 qtyemFSWFLRPLPGPHKQ---LLHHVSTLAAFTVRQVQQHQGNLDASGP--ARDLVDAFLLKMAQEEQNPGTE---FTN 289
Cdd:cd20652 158 -----FLPFLRHLPSYKKAiefLVQGQAKTHAIYQKIIDEHKRRLKPENPrdAEDFELCELEKAKKEGEDRDLFdgfYTD 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 290 KNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPM 369
Cdd:cd20652 233 EQLHHLLADLFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPL 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 370 GIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAE 449
Cdd:cd20652 313 GIPHGCTEDAVLAGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTDGKYLKPEAFIPFQTGKRMCLGDELARMI 392
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 13449277 450 LFLFFTTILQAFSLESPCPPDTLSLKPTVsGLFNIPPAFQL 490
Cdd:cd20652 393 LFLFTARILRKFRIALPDGQPVDSEGGNV-GITLTPPPFKI 432
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
64-458 6.38e-80

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


Pssm-ID: 410768  Cd Length: 434  Bit Score: 255.70  E-value: 6.38e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLALRDLGMG- 141
Cdd:cd20675   1 YGDVFQIRLGS-RPVVVLNGERAIRQALVQQGTDFAGRPDFASFRVVSGGRSLAFGGySERWKAHRRVAHSTVRAFSTRn 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 ---KREGEELIQAEARCLVETF--QGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAvvraaggtLLGVSSQG 216
Cdd:cd20675  80 prtRKAFERHVLGEARELVALFlrKSAGGAYFDPAPPLVVAVANVMSAVCFGKRYSHDDAEFRS--------LLGRNDQF 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 217 GQTY------EMFSWfLRPLPGPHKQLLHHVSTL----AAFTVRQVQQHQGNLDAsGPARDLVDAFLLKM-AQEEQNPGT 285
Cdd:cd20675 152 GRTVgagslvDVMPW-LQYFPNPVRTVFRNFKQLnrefYNFVLDKVLQHRETLRG-GAPRDMMDAFILALeKGKSGDSGV 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 286 EFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLA 365
Cdd:cd20675 230 GLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDRLPCIEDQPNLPYVMAFLYEAMRFSS 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 366 LVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAF--LPFSLGKRVCLGE 443
Cdd:cd20675 310 FVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFLDENGFLNKDLASsvMIFSVGKRRCIGE 389
                       410
                ....*....|....*
gi 13449277 444 GLAKAELFLfFTTIL 458
Cdd:cd20675 390 ELSKMQLFL-FTSIL 403
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
64-490 6.84e-79

cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is pseudogenized in humans because of five nonsense mutations in the putative coding region. However, in other organisms including cynomolgus monkey, CYP1D1 is a functional drug-metabolizing enzyme that is highly expressed in the liver. CYP1D1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410770 [Multi-domain]  Cd Length: 435  Bit Score: 253.09  E-value: 6.84e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN--GERWRQLRKFTMLALRDLGMG 141
Cdd:cd20677   1 YGDVFQIKLG-MLPVVVVSGLETIKQVLLKQGESFAGRPDFYTFSLIANGKSMTFSEkyGESWKLHKKIAKNALRTFSKE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 KREG-------EELIQAEARCLVETF--QGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVV-------RAA 205
Cdd:cd20677  80 EAKSstcscllEEHVCAEASELVKTLveLSKEKGSFDPVSLITCAVANVVCALCFGKRYDHSDKEFLTIVeinndllKAS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 206 GGTLLGvssqggqtyeMFSWFLRPLPGPH-KQLLHHVSTLAAFTVRQVQQHQGNLDASGpARDLVDAfLLKMAQEEQNPG 284
Cdd:cd20677 160 GAGNLA----------DFIPILRYLPSPSlKALRKFISRLNNFIAKSVQDHYATYDKNH-IRDITDA-LIALCQERKAED 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 TE--FTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:cd20677 228 KSavLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFR 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKH--EAFLPFSLGKRVC 440
Cdd:cd20677 308 HSSFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSlvEKVLIFGMGVRKC 387
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 13449277 441 LGEGLAKAELFLFFTTILQAFSLESpCPPDTLSLKPTVsGLFNIPPAFQL 490
Cdd:cd20677 388 LGEDVARNEIFVFLTTILQQLKLEK-PPGQKLDLTPVY-GLTMKPKPYRL 435
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
64-493 1.75e-75

cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), also called steroid 21-hydroxylase (EC 1.14.14.16) or cytochrome P-450c21 or CYP21A2 (in humans), catalyzes the 21-hydroxylation of steroids such as progesterone and 17-alpha-hydroxyprogesterone (17-alpha-OH-progesterone) to form 11-deoxycorticosterone and 11-deoxycortisol, respectively. It is required for the adrenal synthesis of mineralocorticoids and glucocorticoids. Deficiency of this CYP is involved in ~95% of cases of human congenital adrenal hyperplasia, a disorder of adrenal steroidogenesis. There are two CYP21 genes in the human genome, CYP21A1 (a pseudogene) and CYP21A2 (the functional gene). Deficiencies in steroid 21-hydroxylase activity lead to a type of congenital adrenal hyperplasia, which has three clinical forms: a severe form with concurrent defects in both cortisol and aldosterone biosynthesis; a form with adequate aldosterone biosynthesis; and a mild, non-classic form that can be asymptomatic or associated with signs of postpubertal androgen excess without cortisol deficiency. CYP21A2 is also the major autoantigen in autoimmune Addison disease. Cyp21 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410767 [Multi-domain]  Cd Length: 424  Bit Score: 243.86  E-value: 1.75e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTvaMLEGTFD-GHGVFFSNG---ERWRQLRKFTMLALRdLG 139
Cdd:cd20674   1 YGPIYRLRLG-LQDVVVLNSKRTIREALVRKWADFAGRPH--SYTGKLVsQGGQDLSLGdysLLWKAHRKLTRSALQ-LG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 140 MgKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSyEDKEFQAVVRAAGGTLLGVSSQGGQT 219
Cdd:cd20674  77 I-RNSLEPVVEQLTQELCERMRAQAGTPVDIQEEFSLLTCSIICCLTFGDKED-KDTLVQAFHDCVQELLKTWGHWSIQA 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 220 YEMFSwFLRPLPGPH-KQLLHHVSTLAAFTVRQVQQHQGNLDAsGPARDLVDAFLLKMAQEEQNPGT-EFTNKNMLMTVI 297
Cdd:cd20674 155 LDSIP-FLRFFPNPGlRRLKQAVENRDHIVESQLRQHKESLVA-GQWRDMTDYMLQGLGQPRGEKGMgQLLEGHVHMAVV 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 298 YLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMR 377
Cdd:cd20674 233 DLFIGGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPHRTTR 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 378 TTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADgrfRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTI 457
Cdd:cd20674 313 DSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLEPG---AANRALLPFGCGARVCLGEPLARLELFVFLARL 389
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 13449277 458 LQAFSLESPcPPDTL-SLKPTVSGLFNIPPaFQLQVR 493
Cdd:cd20674 390 LQAFTLLPP-SDGALpSLQPVAGINLKVQP-FQVRLQ 424
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
64-476 4.16e-71

cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists of two human members, CYP1A1 and CYP1A2, which overlap in their activities. CYP1A2 is the highly expressed cytochrome enzyme in the human liver, while CYP1A1 is mostly found in extrahepatic tissues. Known common substrates include aromatic compounds such as polycyclic aromatic hydrocarbons, arachidonic acid and eicosapentoic acid, as well as melatonin and 6-hydroxylate melatonin. In addition, CYP1A1 activates procarcinogens into carcinogens via epoxides, and metabolizes heterocyclic aromatic amines of industrial origin. CYP1A2 metabolizes numerous natural products that result in toxic products, such as the transformation of methyleugenol to 1'-hydroxymethyleugenol, estragole to reactive metabolites, and oxidation of nephrotoxins. It also plays an important role in the metabolism of several clinical drugs including analgesics, antipyretics, antipsychotics, antidepressants, anti-inflammatory, and cardiovascular drugs. The CYP1A subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410769 [Multi-domain]  Cd Length: 437  Bit Score: 232.98  E-value: 4.16e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSN--GERWRQLRKFTMLALRDLGMG 141
Cdd:cd20676   1 YGDVLQIQIGS-RPVVVLSGLDTIRQALVKQGDDFKGRPDLYSFRFISDGQSLTFSTdsGPVWRARRKLAQNALKTFSIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 KREG-------EELIQAEARCLVETFQ---GTEGRpFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRaaggtllg 211
Cdd:cd20676  80 SSPTsssscllEEHVSKEAEYLVSKLQelmAEKGS-FDPYRYIVVSVANVICAMCFGKRYSHDDQELLSLVN-------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 212 VSSQGGQTYEM-----FSWFLRPLPGPH-KQLLHHVSTLAAFTVRQVQQHQGNLDaSGPARDLVDAfLLKMAQE---EQN 282
Cdd:cd20676 151 LSDEFGEVAGSgnpadFIPILRYLPNPAmKRFKDINKRFNSFLQKIVKEHYQTFD-KDNIRDITDS-LIEHCQDkklDEN 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 283 PGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:cd20676 229 ANIQLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILETFR 308
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR-FRKHEA--FLPFSLGKRV 439
Cdd:cd20676 309 HSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFLTADGTeINKTESekVMLFGLGKRR 388
                       410       420       430
                ....*....|....*....|....*....|....*..
gi 13449277 440 CLGEGLAKAELFLFFTTILQAFSLESPcPPDTLSLKP 476
Cdd:cd20676 389 CIGESIARWEVFLFLAILLQQLEFSVP-PGVKVDMTP 424
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
65-470 7.26e-67

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


Pssm-ID: 410651 [Multi-domain]  Cd Length: 391  Bit Score: 220.46  E-value: 7.26e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMgkRE 144
Cdd:cd00302   1 GPVFRVRLG-GGPVVVVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRAL--AA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 145 GEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSqggqtyemfs 224
Cdd:cd00302  78 LRPVIREIARELLDRLAAGGEVGDDVADLAQPLALDVIARLLGGPDLGEDLEELAELLEALLKLLGPRLL---------- 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 225 wfLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAfllkmaqeeqNPGTEFTNKNMLMTVIYLLFAGT 304
Cdd:cd00302 148 --RPLPSPRLRRLRRARARLRDYLEELIARRRAEPADDLDLLLLADA----------DDGGGLSDEEIVAELLTLLLAGH 215
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 305 MTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLgdrTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGY 384
Cdd:cd00302 216 ETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTPEDL---SKLPYLEAVVEETLRLYPPVPL-LPRVATEDVELGGY 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 385 TLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKheAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:cd00302 292 TIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRY--AHLPFGAGPHRCLGARLARLELKLALATLLRRFDFE 369

                ....*.
gi 13449277 465 SPCPPD 470
Cdd:cd00302 370 LVPDEE 375
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
65-468 7.18e-56

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: 192.38  E-value: 7.18e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLE-GTFDGHGVFFS-NGERWRQLRKFTMLalrDLGMGK 142
Cdd:cd20618   1 GPLMYLRLGS-VPTVVVSSPEMAKEVLKTQDAVFASRPRTAAGKiFSYNGQDIVFApYGPHWRHLRKICTL---ELFSAK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 R--EGEELIQAEARCLVETF--QGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYED-------KEFQAVVRAAGgTLLG 211
Cdd:cd20618  77 RleSFQGVRKEELSHLVKSLleESESGKPVNLREHLSDLTLNNITRMLFGKRYFGESekeseeaREFKELIDEAF-ELAG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 212 VSSQGGqtyemFSWFLRPLP--GPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLkmaQEEQNPGTEFTN 289
Cdd:cd20618 156 AFNIGD-----YIPWLRWLDlqGYEKRMKKLHAKLDRFLQKIIEEHREKRGESKKGGDDDDDLLL---LLDLDGEGKLSD 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 290 KNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPM 369
Cdd:cd20618 228 DNIKALLLDMLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPL 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 370 GIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAF--LPFSLGKRVCLGEGLAK 447
Cdd:cd20618 308 LLPHESTEDCKVAGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIDDVKGQDFelLPFGSGRRMCPGMPLGL 387
                       410       420
                ....*....|....*....|.
gi 13449277 448 AELFLFFTTILQAFSLESPCP 468
Cdd:cd20618 388 RMVQLTLANLLHGFDWSLPGP 408
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
64-488 2.68e-55

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: 190.87  E-value: 2.68e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLE--GTFDGHGVFFSNGERWRQLRKFTMLALRdlGMG 141
Cdd:cd11065   1 YGPIISLKVG-GQTIIVLNSPKAAKDLLEKRSAIYSSRPRMPMAGelMGWGMRLLLMPYGPRWRLHRRLFHQLLN--PSA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 KREGEELIQAEAR-CLVETFQgtegRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQTY 220
Cdd:cd11065  78 VRKYRPLQELESKqLLRDLLE----SPDDFLDHIRRYAASIILRLAYGYRVPSYDDPLLRDAEEAMEGFSEAGSPGAYLV 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 221 EMFSwFLRPLP-----GPHKQLLHHVSTLAAFTVRQVQQHQGNLdASGPARD-LVDAFLLKMAQEEQnpGTEFTNKNMLM 294
Cdd:cd11065 154 DFFP-FLRYLPswlgaPWKRKARELRELTRRLYEGPFEAAKERM-ASGTATPsFVKDLLEELDKEGG--LSEEEIKYLAG 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 295 TVIYllfAGTMTVSTTVgYTLLLLM-KYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPR 373
Cdd:cd11065 230 SLYE---AGSDTTASTL-QTFILAMaLHPEVQKKAQEELDRVVGPDRLPTFEDRPNLPYVNAIVKEVLRWRPVAPLGIPH 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 374 TLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR--FRKHEAFLPFSLGKRVCLGEGLAKAELF 451
Cdd:cd11065 306 ALTEDDEYEGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYLDDPKGtpDPPDPPHFAFGFGRRICPGRHLAENSLF 385
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 13449277 452 LFFTTILQAFSLESPCPPDTLSLKPTV---SGLFNIPPAF 488
Cdd:cd11065 386 IAIARLLWAFDIKKPKDEGGKEIPDEPeftDGLVSHPLPF 425
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
59-464 1.94e-49

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: 175.08  E-value: 1.94e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  59 RLSKKYGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRdl 138
Cdd:cd11053   6 RLRARYGDVFTLRVPGLGPVVVLSDPEAIKQIFTADPDVLHPGEGNSLLEPLLGPNSLLLLDGDRHRRRRKLLMPAFH-- 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 139 gmGKREG--EELIQAEARCLVETFQgtEGRPFDPSLLLAQATSNVVCSLLFGLrfsyEDKEFQAVVRAAGGTLLGVSSQG 216
Cdd:cd11053  84 --GERLRayGELIAEITEREIDRWP--PGQPFDLRELMQEITLEVILRVVFGV----DDGERLQELRRLLPRLLDLLSSP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 217 GQTYEMFSWFLRPlPGPHKQLLHHVSTLAAFTVRQVQQHQgnlDASGPARDLVDAFLLKmAQEEQnpGTEFTNKNM---L 293
Cdd:cd11053 156 LASFPALQRDLGP-WSPWGRFLRARRRIDALIYAEIAERR---AEPDAERDDILSLLLS-ARDED--GQPLSDEELrdeL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 294 MTviyLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNrelGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPR 373
Cdd:cd11053 229 MT---LLFAGHETTATALAWAFYWLHRHPEVLARLLAELD---ALGGDPDPEDIAKLPYLDAVIKETLRLYPVAPL-VPR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 374 TLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDAdgRFRKHEaFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd11053 302 RVKEPVELGGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGR--KPSPYE-YLPFGGGVRRCIGAAFALLEMKVV 378
                       410
                ....*....|.
gi 13449277 454 FTTILQAFSLE 464
Cdd:cd11053 379 LATLLRRFRLE 389
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
65-478 2.36e-48

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: 172.32  E-value: 2.36e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPWrPVVVLVGQEAVREALGGQaeEFSGRGTV-AMLEGTFdGHGVFFSNGERWRQLRK-------FTMLalr 136
Cdd:cd20628   1 GGVFRLWIGPK-PYVVVTNPEDIEVILSSS--KLITKSFLyDFLKPWL-GDGLLTSTGEKWRKRRKlltpafhFKIL--- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 137 dlgmgkrEG-EELIQAEARCLVETFQGTEGRP-FDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVss 214
Cdd:cd20628  74 -------ESfVEVFNENSKILVEKLKKKAGGGeFDIFPYISLCTLDIICETAMGVKLNAQSNEDSEYVKAVKRILEII-- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 215 qggqTYEMFSWFLRP-----LPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVD--------AFL--LKMAQE 279
Cdd:cd20628 145 ----LKRIFSPWLRFdfifrLTSLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEEDDefgkkkrkAFLdlLLEAHE 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 280 EQNPgteFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELG-AGQAPSLGDRTRLPYTDAVLH 358
Cdd:cd20628 221 DGGP---LTDEDIREEVDTFMFAGHDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGdDDRRPTLEDLNKMKYLERVIK 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 359 EAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKR 438
Cdd:cd20628 298 ETLRLYPSVPF-IGRRLTEDIKLDGYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAKRHPYAYIPFSAGPR 376
                       410       420       430       440
                ....*....|....*....|....*....|....*....|
gi 13449277 439 VCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTV 478
Cdd:cd20628 377 NCIGQKFAMLEMKTLLAKILRNFRVLPVPPGEDLKLIAEI 416
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
65-477 1.69e-47

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: 169.30  E-value: 1.69e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFdGHGVFFSNGERWRQLRK-----FTMLALRDLG 139
Cdd:cd20620   1 GDVVRLRLGP-RRVYLVTHPDHIQHVLVTNARNYVKGGVYERLKLLL-GNGLLTSEGDLWRRQRRlaqpaFHRRRIAAYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 140 mgkregeELIQAEARCLVETFQGTEGR-PFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLlgvssqggq 218
Cdd:cd20620  79 -------DAMVEATAALLDRWEAGARRgPVDVHAEMMRLTLRIVAKTLFGTDVEGEADEIGDALDVALEYA--------- 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 219 TYEMFSWFLRPL---PGPHKQLLHHVSTLAAFTVRQVQQHQgnldASGPARDLVDAFLLKMAQEEQnpGTEFTNKNMLMT 295
Cdd:cd20620 143 ARRMLSPFLLPLwlpTPANRRFRRARRRLDEVIYRLIAERR----AAPADGGDLLSMLLAARDEET--GEPMSDQQLRDE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 296 VIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGaGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTL 375
Cdd:cd20620 217 VMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG-GRPPTAEDLPQLPYTEMVLQESLRLYPPAWI-IGREA 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 376 MRTTRFRGYTLPQGTEVF--PLLgsILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd20620 295 VEDDEIGGYRIPAGSTVLisPYV--THRDPRFWPDPEAFDPERFTPEREAARPRYAYFPFGGGPRICIGNHFAMMEAVLL 372
                       410       420
                ....*....|....*....|....*....
gi 13449277 454 FTTILQAFSLE-----SPCPPDTLSLKPT 477
Cdd:cd20620 373 LATIAQRFRLRlvpgqPVEPEPLITLRPK 401
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
49-477 2.03e-44

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


Pssm-ID: 225035 [Multi-domain]  Cd Length: 411  Bit Score: 161.44  E-value: 2.03e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  49 RPGALYSGLMRLSKKYGPVFTIYL-GPWRPVVVLVGQEAVREALGgQAEEFSGRGTVAM----LEGTFDGHGVFFSNGER 123
Cdd:COG2124  20 LEFAPRFFLERAEDPYGDYFTLRLpGPGDGFWVVSRPADVREVLR-DPRFFSSALGAGLrprlLRPVLGDGSLLTLDGPE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 124 WRQLRKFTMLALRdlGMGKREGEELIQAEARCLVETFQGteGRPFDPSLLLAQATSNVVCSLlFGLRFSYEDKEFQAVVR 203
Cdd:COG2124  99 HTRLRKLLAPAFT--PRALRGYRPLIREIADRLLDDLWQ--GGADLVLDFAAELTLRVIAEL-LGVPLEDRPQLLRWSDA 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 204 AAggtllgvssqggqtyeMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNldasgPARDLVDAfllkMAQEEQNP 283
Cdd:COG2124 174 LL----------------LRLDPDLGPEEPWRRARAARRELDAYLRALIAERRAA-----PRDDLLSL----LLSAEDDG 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 284 GTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRelgagqapslgdrtrlPYTDAVLHEAQRL 363
Cdd:COG2124 229 GGRLSDDEIRDELITLLVAGHETTANALAWALYALLRHPDQLAKLRAEPDR----------------PLLEAVVEETLRL 292
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 364 LALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFldadgrfrkHEAFLPFSLGKRVCLGE 443
Cdd:COG2124 293 YPPVPL-ARRVATEDVELGGYRIPAGTVVLLSIGAANRDPEVFPDPDEFDPERF---------NNAHLPFGGGPHRCLGA 362
                       410       420       430
                ....*....|....*....|....*....|....
gi 13449277 444 GLAKAELFLFFTTILQAFSLESPCPPDTLSLKPT 477
Cdd:COG2124 363 ALARLELKVALAELLRRFPLLLLAEPPPLVRRPT 396
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
63-481 5.02e-44

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: 160.44  E-value: 5.02e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDgHGVFFSNGERWRQLRK-----FTMLALRd 137
Cdd:cd11055   1 KYGKVFGLYFGT-IPVIVVSDPEMIKEILVKEFSNFTNRPLFILLDEPFD-SSLLFLKGERWKRLRTtlsptFSSGKLK- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 138 lGMgkregEELIQAEARCLVETF--QGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQ 215
Cdd:cd11055  78 -LM-----VPIINDCCDELVEKLekAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQNNPDDPFLKAAKKIFRNSIIR 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 216 GGQTYEMFSW----FLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQgnldaSGPARDLVDAFLLKMAQEEQNPGTEFTNKN 291
Cdd:cd11055 152 LFLLLLLFPLrlflFLLFPFVFGFKSFSFLEDVVKKIIEQRRKNK-----SSRRKDLLQLMLDAQDSDEDVSKKKLTDDE 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 292 MLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgI 371
Cdd:cd11055 227 IVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEIDEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFF-I 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 372 PRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELF 451
Cdd:cd11055 306 SRECKEDCTINGVFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERFSPENKAKRHPYAYLPFGAGPRNCIGMRFALLEVK 385
                       410       420       430
                ....*....|....*....|....*....|
gi 13449277 452 LFFTTILQAFSLEsPCPPDTLSLKPTVSGL 481
Cdd:cd11055 386 LALVKILQKFRFV-PCKETEIPLKLVGGAT 414
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
115-485 8.74e-43

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: 157.30  E-value: 8.74e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 115 GVFFSNGERWRQLRKftmlALRDLGMGKRE-----------GEELIQ------AEARCLVETFQ------GTEGrpfdps 171
Cdd:cd11054  57 GLLNSNGEEWHRLRS----AVQKPLLRPKSvasylpainevADDFVErirrlrDEDGEEVPDLEdelykwSLES------ 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 172 lllaqatsnvVCSLLFGLRF----SYEDKEFQAVVRAAGGTLlgvSSQGGQTYEMFSWFLRPLPgPHKQLLHHVSTLAAF 247
Cdd:cd11054 127 ----------IGTVLFGKRLgcldDNPDSDAQKLIEAVKDIF---ESSAKLMFGPPLWKYFPTP-AWKKFVKAWDTIFDI 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 248 TVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEqnpgtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKW 327
Cdd:cd11054 193 ASKYVDEALEELKKKDEEDEEEDSLLEYLLSKP-----GLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEK 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 328 VREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPmGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFK 407
Cdd:cd11054 268 LYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAP-GNGRILPKDIVLSGYHIPKGTLVVLSNYVMGRDEEYFP 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 408 HPEEFNPDRFLDADGRFRKHEAF--LPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPdtlsLKPTVSgLFNIP 485
Cdd:cd11054 347 DPEEFIPERWLRDDSENKNIHPFasLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEYHHEE----LKVKTR-LILVP 421
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
63-452 2.49e-42

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: 156.08  E-value: 2.49e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGR-GTVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLALrdLGM 140
Cdd:cd11072   1 KYGPLMLLRLGS-VPTVVVSSPEAAKEVLKTHDLVFASRpKLLAARILSYGGKDIAFAPyGEYWRQMRKICVLEL--LSA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 141 GK-------REgEELiqaeARcLVETFQGTEG--RPFDPSLLLAQATSNVVCSLLFGLRFSYEDKE-FQAVVRAAGgTLL 210
Cdd:cd11072  78 KRvqsfrsiRE-EEV----SL-LVKKIRESASssSPVNLSELLFSLTNDIVCRAAFGRKYEGKDQDkFKELVKEAL-ELL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 211 GVSSQGgqtyEMFSW--FLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNlDASGPARDLVDAFLLKMAQEEQNPGTEFT 288
Cdd:cd11072 151 GGFSVG----DYFPSlgWIDLLTGLDRKLEKVFKELDAFLEKIIDEHLDK-KRSKDEDDDDDDLLDLRLQKEGDLEFPLT 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 289 NKN---MLMTVIyllFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLA 365
Cdd:cd11072 226 RDNikaIILDMF---LAGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLRLHP 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 366 LVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFR-KHEAFLPFSLGKRVC--LG 442
Cdd:cd11072 303 PAPLLLPRECREDCKINGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIDFKgQDFELIPFGAGRRICpgIT 382
                       410
                ....*....|
gi 13449277 443 EGLAKAELFL 452
Cdd:cd11072 383 FGLANVELAL 392
PTZ00404 PTZ00404
cytochrome P450; Provisional
54-465 2.76e-41

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 154.11  E-value: 2.76e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   54 YSGLMRLSKKYGPVFTIYLGPWRpVVVLVGQEAVREALGGQAEEFSGRGTVAMLE-GTFdGHGVFFSNGERWRQLRKFTM 132
Cdd:PTZ00404  51 HRDLTKMSKKYGGIFRIWFADLY-TVVLSDPILIREMFVDNFDNFSDRPKIPSIKhGTF-YHGIVTSSGEYWKRNREIVG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  133 LALRDLGMgkREGEELIQAEARCLVETFQGTE--GRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKefqaVVRAAGGTLL 210
Cdd:PTZ00404 129 KAMRKTNL--KHIYDLLDDQVDVLIESMKKIEssGETFEPRYYLTKFTMSAMFKYIFNEDISFDED----IHNGKLAELM 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  211 GVSSQGGQTYEMFSWF-----LRPLPgpHKQLLH---HVSTLAAFTVRQVQQHQGNLDASGPaRDLVDaFLLKmaqeEQN 282
Cdd:PTZ00404 203 GPMEQVFKDLGSGSLFdvieiTQPLY--YQYLEHtdkNFKKIKKFIKEKYHEHLKTIDPEVP-RDLLD-LLIK----EYG 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  283 PGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:PTZ00404 275 TNTDDDILSILATILDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLR 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  363 LLALVPMGIPRTLMR-TTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADgrfrKHEAFLPFSLGKRVCL 441
Cdd:PTZ00404 355 YKPVSPFGLPRSTSNdIIIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD----SNDAFMPFSIGPRNCV 430
                        410       420
                 ....*....|....*....|....
gi 13449277  442 GEGLAKAELFLFFTTILQAFSLES 465
Cdd:PTZ00404 431 GQQFAQDELYLAFSNIILNFKLKS 454
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
61-470 4.87e-40

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


Pssm-ID: 410696 [Multi-domain]  Cd Length: 435  Bit Score: 149.99  E-value: 4.87e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  61 SKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRG-TVAMLEGTFDGHGVFF-SNGERWRQLRK------FT- 131
Cdd:cd11073   1 AKKYGPIMSLKLGS-KTTVVVSSPEAAREVLKTHDRVLSGRDvPDAVRALGHHKSSIVWpPYGPRWRMLRKicttelFSp 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 132 -ML-ALRDLGMgkREGEELIQaearcLVETFQGtEGRPFDPSLLLAQATSNVVCSLLFGLRFSYED----KEFQAVVRAA 205
Cdd:cd11073  80 kRLdATQPLRR--RKVRELVR-----YVREKAG-SGEAVDIGRAAFLTSLNLISNTLFSVDLVDPDsesgSEFKELVREI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 206 GgTLLG---VSSqggqtyemFSWFLRP--LPGPHKQLLHHVSTLAAFTVRQVQQHQGNlDASGPARDLVDAFLLKMAQEE 280
Cdd:cd11073 152 M-ELAGkpnVAD--------FFPFLKFldLQGLRRRMAEHFGKLFDIFDGFIDERLAE-REAGGDKKKDDDLLLLLDLEL 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 281 QNPgTEFTN---KNMLMTviyLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVL 357
Cdd:cd11073 222 DSE-SELTRnhiKALLLD---LFVAGTDTTSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVV 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 358 HEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFR-KHEAFLPFSLG 436
Cdd:cd11073 298 KETLRLHPPAPLLLPRKAEEDVEVMGYTIPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDFKgRDFELIPFGSG 377
                       410       420       430
                ....*....|....*....|....*....|....
gi 13449277 437 KRVCLGEGLAKAELFLFFTTILQAFSLESPCPPD 470
Cdd:cd11073 378 RRICPGLPLAERMVHLVLASLLHSFDWKLPDGMK 411
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
63-461 1.36e-36

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: 140.07  E-value: 1.36e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGR----GTVAMLegTFDGHGVFFSN-GERWRQLRK-FT--ML- 133
Cdd:cd11075   1 KYGPIFTLRMG-SRPLIVVASRELAHEALVQKGSSFASRppanPLRVLF--SSNKHMVNSSPyGPLWRTLRRnLVseVLs 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 134 --------ALRDLGMGKregeeliqaearcLVETFQGTEGRPFDPSLLLAQATSNVVCSLL---FGLRFsyEDKEFQAVV 202
Cdd:cd11075  78 psrlkqfrPARRRALDN-------------LVERLREEAKENPGPVNVRDHFRHALFSLLLymcFGERL--DEETVRELE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 203 RAAGGTLLgvssqggqTYEMFSWF-----LRPLPGphKQLLHHVSTLaafTVRQV--------QQHQGNLDASGPARDLV 269
Cdd:cd11075 143 RVQRELLL--------SFTDFDVRdffpaLTWLLN--RRRWKKVLEL---RRRQEevllplirARRKRRASGEADKDYTD 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 270 DAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTR 349
Cdd:cd11075 210 FLLLDLLDLKEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEEDLPK 289
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 350 LPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADG------- 422
Cdd:cd11075 290 MPYLKAVVLETLRRHPPGHFLLPHAVTEDTVLGGYDIPAGAEVNFNVAAIGRDPKVWEDPEEFKPERFLAGGEaadidtg 369
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 13449277 423 --RFRkheaFLPFSLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd11075 370 skEIK----MMPFGAGRRICPGLGLATLHLELFVARLVQEF 406
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
65-469 3.16e-36

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


Pssm-ID: 410704 [Multi-domain]  Cd Length: 421  Bit Score: 138.99  E-value: 3.16e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSgrgTVAMLEGTFD---GHGVFFSNGERWRQLRKFTMLALRDLGMg 141
Cdd:cd11083   1 GSAYRFRLGR-QPVLVISDPELIREVLRRRPDEFR---RISSLESVFRemgINGVFSAEGDAWRRQRRLVMPAFSPKHL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 kREGEELIQAEARCLVETFQ--GTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQGGQT 219
Cdd:cd11083  76 -RYFFPTLRQITERLRERWEraAAEGEAVDVHKDLMRYTVDVTTSLAFGYDLNTLERGGDPLQEHLERVFPMLNRRVNAP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 220 YEMFSWFLRPlpgPHKQLLHHVSTLAAFTVRQVQQHQGNLDAsGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYL 299
Cdd:cd11083 155 FPYWRYLRLP---ADRALDRALVEVRALVLDIIAAARARLAA-NPALAEAPETLLAMMLAEDDPDARLTDDEIYANVLTL 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 300 LFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELG-AGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRT 378
Cdd:cd11083 231 LLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGgARVPPLLEALDRLPYLEAVARETLRLKPVAPL-LFLEPNED 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 379 TRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHE--AFLPFSLGKRVCLGEGLAKAELFLFFTT 456
Cdd:cd11083 310 TVVGDIALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEPHDpsSLLPFGAGPRLCPGRSLALMEMKLVFAM 389
                       410
                ....*....|...
gi 13449277 457 ILQAFSLESPCPP 469
Cdd:cd11083 390 LCRNFDIELPEPA 402
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
64-468 9.26e-36

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: 137.39  E-value: 9.26e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPWrPVVVLVGQEAVREALGGQAEeFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMGKR 143
Cdd:cd11049  12 HGDLVRIRLGPR-PAYVVTSPELVRQVLVNDRV-FDKGGPLFDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 144 EgeELIQAEARCLVETFQgtEGRPFDPSLLLAQATSNVVCSLLFGLRFsyeDKEFQAVVRAAGGTLLGVssqggqTYEMF 223
Cdd:cd11049  90 A--EVMREEAEALAGSWR--PGRVVDVDAEMHRLTLRVVARTLFSTDL---GPEAAAELRQALPVVLAG------MLRRA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SW--FLRPLPGP-----HKQL--LHHVSTLAAFTVRQVQQHQGNLDAsgpardlvdafLLKMAQEEQNPGteFTNKNMLM 294
Cdd:cd11049 157 VPpkFLERLPTPgnrrfDRALarLRELVDEIIAEYRASGTDRDDLLS-----------LLLAARDEEGRP--LSDEELRD 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 295 TVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGaGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRT 374
Cdd:cd11049 224 QVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDAVLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWL-LTRR 301
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 375 LMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFL-DADGRFRKHeAFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd11049 302 TTADVELGGHRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRWLpGRAAAVPRG-AFIPFGAGARKCIGDTFALTELTLA 380
                       410
                ....*....|....*
gi 13449277 454 FTTILQAFSLEsPCP 468
Cdd:cd11049 381 LATIASRWRLR-PVP 394
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
63-485 4.26e-35

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: 136.13  E-value: 4.26e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRK-----FTMLALRD 137
Cdd:cd11056   1 GGEPFVGIYLF-RRPALLVRDPELIKQILVKDFAHFHDRGLYSDEKDDPLSANLFSLDGEKWKELRQkltpaFTSGKLKN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 138 L-GMGKREGEELI-----QAEARCLVETFQgtegrpfdpslLLAQATSNVVCSLLFGLR---FSYEDKEFQAVVRAAggt 208
Cdd:cd11056  80 MfPLMVEVGDELVdylkkQAEKGKELEIKD-----------LMARYTTDVIASCAFGLDansLNDPENEFREMGRRL--- 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 209 llgVSSQGGQTYEMFSWFLRPLPGPHKQLLHHVSTLAAF---TVRQ-VQQHQGNldasGPAR-DLVDaFLLKMAQEEQNP 283
Cdd:cd11056 146 ---FEPSRLRGLKFMLLFFFPKLARLLRLKFFPKEVEDFfrkLVRDtIEYREKN----NIVRnDFID-LLLELKKKGKIE 217
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 284 GT----EFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAP----SLGDrtrLPYTDA 355
Cdd:cd11056 218 DDksekELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREEIDEVLEKHGGEltyeALQE---MKYLDQ 294
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 356 VLHEAQRLLALVPMgiprtLMRTTR------FRGYTLPQGTEVF-PLLGsILHDPNIFKHPEEFNPDRFLDADGRFRKHE 428
Cdd:cd11056 295 VVNETLRKYPPLPF-----LDRVCTkdytlpGTDVVIEKGTPVIiPVYA-LHHDPKYYPEPEKFDPERFSPENKKKRHPY 368
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13449277 429 AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLEsPCPPDTLSLKPTVSGLFNIP 485
Cdd:cd11056 369 TYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVE-PSSKTKIPLKLSPKSFVLSP 424
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
62-464 1.50e-34

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: 134.33  E-value: 1.50e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  62 KKYGPVF-TIYLGpwRPVVVLVGQEAVREALGGQAEEFSGrGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGM 140
Cdd:cd11044  19 QKYGPVFkTHLLG--RPTVFVIGAEAVRFILSGEGKLVRY-GWPRSVRRLLGENSLSLQDGEEHRRRRKLLAPAFSREAL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 141 GkrEGEELIQAEARCLVETFQGTEGRPFDPSLllAQATSNVVCSLLFGLRfSYEDKEfqavvraaggtllgvssQGGQTY 220
Cdd:cd11044  96 E--SYVPTIQAIVQSYLRKWLKAGEVALYPEL--RRLTFDVAARLLLGLD-PEVEAE-----------------ALSQDF 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 221 EMFS--WFLRPLPGP----------HKQLLHHVSTLaaftVRQvQQHQGNLDASgpardlvDA-FLLKMAQEEQnpGTEF 287
Cdd:cd11044 154 ETWTdgLFSLPVPLPftpfgrairaRNKLLARLEQA----IRE-RQEEENAEAK-------DAlGLLLEAKDED--GEPL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 288 TNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALV 367
Cdd:cd11044 220 SMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQ-DALGLEEPLTLESLKKMPYLDQVIKEVLRLVPPV 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 368 PMGIpRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHE-AFLPFSLGKRVCLGEGLA 446
Cdd:cd11044 299 GGGF-RKVLEDFELGGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPARSEDKKKPfSLIPFGGGPRECLGKEFA 377
                       410
                ....*....|....*...
gi 13449277 447 KAELFLFFTTILQAFSLE 464
Cdd:cd11044 378 QLEMKILASELLRNYDWE 395
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
164-468 5.02e-34

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: 133.09  E-value: 5.02e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 164 EGRPFDPSLLLAQATSNVVCSLLFGLRFSY--EDKEFQAVVrAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHHV 241
Cdd:cd11060  97 SGKEVDLGKWLQYFAFDVIGEITFGKPFGFleAGTDVDGYI-ASIDKLLPYFAVVGQIPWLDRLLLKNPLGPKRKDKTGF 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 242 STLAAFTVRQVQQHQGNLDASGPAR-DLVDAFLlkmaQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMK 320
Cdd:cd11060 176 GPLMRFALEAVAERLAEDAESAKGRkDMLDSFL----EAGLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLK 251
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 321 YPHVQKWVREEL---NRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPR-------TLmrttrfRGYTLPQGT 390
Cdd:cd11060 252 NPRVYAKLRAEIdaaVAEGKLSSPITFAEAQKLPYLQAVIKEALRLHPPVGLPLERvvppggaTI------CGRFIPGGT 325
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 391 EVFPLLGSILHDPNIF-KHPEEFNPDRFLDADG-RFRKHE-AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPC 467
Cdd:cd11060 326 IVGVNPWVIHRDKEVFgEDADVFRPERWLEADEeQRRMMDrADLTFGAGSRTCLGKNIALLELYKVIPELLRRFDFELVD 405

                .
gi 13449277 468 P 468
Cdd:cd11060 406 P 406
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
57-466 6.31e-34

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221  Cd Length: 503  Bit Score: 134.09  E-value: 6.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   57 LMRLSKKYGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEgTFDGHG---VFFSNGERWRQLRK---- 129
Cdd:PLN02394  56 LAEMAKKYGDVFLLRMG-QRNLVVVSSPELAKEVLHTQGVEFGSRTRNVVFD-IFTGKGqdmVFTVYGDHWRKMRRimtv 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  130 --FTMLALRDlgmgKREGEEliqAEARCLVETFQG-----TEGRPFDPSLLLAqaTSNVVCSLLFGLRF-SYEDKEFqav 201
Cdd:PLN02394 134 pfFTNKVVQQ----YRYGWE---EEADLVVEDVRAnpeaaTEGVVIRRRLQLM--MYNIMYRMMFDRRFeSEDDPLF--- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  202 VRAAGgtLLGVSSQGGQTYEM----FSWFLRPLPGPHKQLLHHVST--LAAFTVRQVQQHQGNLDASGPARDLVDAFLLK 275
Cdd:PLN02394 202 LKLKA--LNGERSRLAQSFEYnygdFIPILRPFLRGYLKICQDVKErrLALFKDYFVDERKKLMSAKGMDKEGLKCAIDH 279
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  276 MAQEEQNpgTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDA 355
Cdd:PLN02394 280 ILEAQKK--GEINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQA 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  356 VLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR-------FRkhe 428
Cdd:PLN02394 358 VVKETLRLHMAIPLLVPHMNLEDAKLGGYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKveangndFR--- 434
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 13449277  429 aFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN02394 435 -FLPFGVGRRSCPGIILALPILGIVLGRLVQNFELLPP 471
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
65-496 7.13e-34

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: 132.39  E-value: 7.13e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAeefsgrgtvaMLEGTFD--------GHGVFFSNGERWRQLRKftMLA-- 134
Cdd:cd20660   1 GPIFRIWLGP-KPIVVLYSAETVEVILSSSK----------HIDKSFEydflhpwlGTGLLTSTGEKWHSRRK--MLTpt 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 135 -----LRDLgmgkregEELIQAEARCLVETFQG-TEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGT 208
Cdd:cd20660  68 fhfkiLEDF-------LDVFNEQSEILVKKLKKeVGKEEFDIFPYITLCALDIICETAMGKSVNAQQNSDSEYVKAVYRM 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 209 LLGVSSQGGQTYeMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAF----------LLKMAQ 278
Cdd:cd20660 141 SELVQKRQKNPW-LWPDFIYSLTPDGREHKKCLKILHGFTNKVIQERKAELQKSLEEEEEDDEDadigkrkrlaFLDLLL 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 279 EEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAG-QAPSLGDRTRLPYTDAVL 357
Cdd:cd20660 220 EASEEGTKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDLKEMKYLECVI 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 358 HEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGK 437
Cdd:cd20660 300 KEALRLFPSVPM-FGRTLSEDIEIGGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAGRHPYAYIPFSAGP 378
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13449277 438 RVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLslkptvsglfniPPAFQLQVRPTD 496
Cdd:cd20660 379 RNCIGQKFALMEEKVVLSSILRNFRIESVQKREDL------------KPAGELILRPVD 425
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
62-469 2.14e-33

cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome P450 51 (CYP51 or sterol 14alpha-demethylase) and related cytochrome P450s. CYP51 is the only cytochrome P450 enzyme with a conserved function across animals, fungi, and plants, in the synthesis of essential sterols. In mammals, it is expressed in many different tissues, with highest expression in testis, ovary, adrenal gland, prostate, liver, kidney, and lung. In fungi, CYP51 is a significant drug target for treatment of human protozoan infections. In plants, it functions within a specialized defense-related metabolic pathway. CYP51 is also found in several bacterial species. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410668 [Multi-domain]  Cd Length: 416  Bit Score: 130.80  E-value: 2.14e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  62 KKYGPVFTIYLGPWRpVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRdlgMG 141
Cdd:cd11042   3 KKYGDVFTFNLLGKK-VTVLLGPEANEFFFNGKDEDLSAEEVYGFLTPPFGGGVVYYAPFAEQKEQLKFGLNILR---RG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 KREGE-ELIQAEARCLVETFqGTEGrPFDpsllLAQATSNVV----CSLLFGLRFSYE-DKEF-QAVVRAAGGTLLgvss 214
Cdd:cd11042  79 KLRGYvPLIVEEVEKYFAKW-GESG-EVD----LFEEMSELTiltaSRCLLGKEVRELlDDEFaQLYHDLDGGFTP---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 215 qggqtyemFSWFLRPLPGPHKQLLHHVST-LAAFTVRQVQQHQGNLDASGpaRDLVDAFllkMAQEEQNpGTEFTNK--- 290
Cdd:cd11042 149 --------IAFFFPPLPLPSFRRRDRARAkLKEIFSEIIQKRRKSPDKDE--DDMLQTL---MDAKYKD-GRPLTDDeia 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 291 NMLmtvIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELG-AGQAPSLGDRTRLPYTDAVLHEAQRLLALVPM 369
Cdd:cd11042 215 GLL---IALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGdGDDPLTYDVLKEMPLLHACIKETLRLHPPIHS 291
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 370 giprtLMRTTR------FRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHE--AFLPFSLGKRVCL 441
Cdd:cd11042 292 -----LMRKARkpfeveGGGYVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKGGkfAYLPFGAGRHRCI 366
                       410       420       430
                ....*....|....*....|....*....|.
gi 13449277 442 GEGLAKAELFLFFTTILQAFSLE---SPCPP 469
Cdd:cd11042 367 GENFAYLQIKTILSTLLRNFDFElvdSPFPE 397
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
143-474 2.40e-32

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: 128.11  E-value: 2.40e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATS----NVVCSLLFGLRF---SYEDKEFQAVVRAAGGTLLGVssq 215
Cdd:cd11061  71 RGYEPRILSHVEQLCEQLDDRAGKPVSWPVDMSDWFNylsfDVMGDLAFGKSFgmlESGKDRYILDLLEKSMVRLGV--- 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 216 GGQTYEMFSWFLRPLPGPhkQLLHHVSTLAAFTVRQVQQHQGNldASGPARDLVdAFLLkmAQEEQNPGTEFTNKNMLMT 295
Cdd:cd11061 148 LGHAPWLRPLLLDLPLFP--GATKARKRFLDFVRAQLKERLKA--EEEKRPDIF-SYLL--EAKDPETGEGLDLEELVGE 220
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 296 VIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDR-TRLPYTDAVLHEAQRLLALVPMGIPR- 373
Cdd:cd11061 221 ARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIRLGPKlKSLPYLRACIDEALRLSPPVPSGLPRe 300
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 374 ------TLMrttrfrGYTLPQGTEVF-PLLgSILHDPNIFKHPEEFNPDRFLDADGRFRKHE-AFLPFSLGKRVCLGEGL 445
Cdd:cd11061 301 tppgglTID------GEYIPGGTTVSvPIY-SIHRDERYFPDPFEFIPERWLSRPEELVRARsAFIPFSIGPRGCIGKNL 373
                       330       340
                ....*....|....*....|....*....
gi 13449277 446 AKAELFLFFTTILQAFSLESPCPPDTLSL 474
Cdd:cd11061 374 AYMELRLVLARLLHRYDFRLAPGEDGEAG 402
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
67-464 2.66e-32

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: 128.06  E-value: 2.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  67 VFTIYLGPWRPVVVLVGQEAVREALggQAEEFSGRGTVAMLEGtFDGHGVFFSNGERWRQLRK-----FTMLALRD-LGM 140
Cdd:cd20659   3 AYVFWLGPFRPILVLNHPDTIKAVL--KTSEPKDRDSYRFLKP-WLGDGLLLSNGKKWKRNRRlltpaFHFDILKPyVPV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 141 GKREGEELI-----QAEARCLVETFQgtegrpfDPSLLlaqaTSNVV--CSllfglrFSYEDKEFQavvraaggtllgvs 213
Cdd:cd20659  80 YNECTDILLekwskLAETGESVEVFE-------DISLL----TLDIIlrCA------FSYKSNCQQ-------------- 128
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 214 sQGGQ------TYEMFS-WFLRplpgpHKQLLHHVSTLAAFT---------VRQVQQH------------QGNLDASGPA 265
Cdd:cd20659 129 -TGKNhpyvaaVHELSRlVMER-----FLNPLLHFDWIYYLTpegrrfkkaCDYVHKFaeeiikkrrkelEDNKDEALSK 202
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 266 RDLVDaFL--LKMAQEEQnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPS 343
Cdd:cd20659 203 RKYLD-FLdiLLTARDED--GKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIE 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 LGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR 423
Cdd:cd20659 280 WDDLSKLPYLTMCIKESLRLYPPVPF-IARTLTKPITIDGVTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIK 358
                       410       420       430       440
                ....*....|....*....|....*....|....*....|.
gi 13449277 424 FRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:cd20659 359 KRDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFELS 399
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
60-476 4.19e-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: 127.64  E-value: 4.19e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  60 LSKKYGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGR--GTVAMLEGT-FDGHG-VFFSNGERWRQLRK-----F 130
Cdd:cd20613   7 WAKEYGPVFVFWIL-HRPIVVVSDPEAVKEVLITLNLPKPPRvySRLAFLFGErFLGNGlVTEVDHEKWKKRRAilnpaF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 131 TMLALRDLgMGK--REGEELIQ-----AEARCLVETFQgtegrpfdpslLLAQATSNVVCSLLFGLRFSY---EDKEFqa 200
Cdd:cd20613  86 HRKYLKNL-MDEfnESADLLVEklskkADGKTEVNMLD-----------EFNRVTLDVIAKVAFGMDLNSiedPDSPF-- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 201 vVRAAGGTLLGVSSQggqtyeMFSWFLRPLPGP---HKQLLHHVSTLAAFTVRQVQQHQGNL-DASGPARDLVdAFLLKM 276
Cdd:cd20613 152 -PKAISLVLEGIQES------FRNPLLKYNPSKrkyRREVREAIKFLRETGRECIEERLEALkRGEEVPNDIL-THILKA 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 277 AQEEQNPGTEftnkNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAV 356
Cdd:cd20613 224 SEEEPDFDME----ELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQV 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 357 LHEAQRLLALVPmGIPRTLMRTTRFRGYTLPQGTEV---FPLLGsilHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPF 433
Cdd:cd20613 300 LKETLRLYPPVP-GTSRELTKDIELGGYKIPAGTTVlvsTYVMG---RMEEYFEDPLKFDPERFSPEAPEKIPSYAYFPF 375
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*...
gi 13449277 434 SLGKRVCLGEGLAKAELFLFFTTILQAFSLE-----SPCPPDTLSLKP 476
Cdd:cd20613 376 SLGPRSCIGQQFAQIEAKVILAKLLQNFKFElvpgqSFGILEEVTLRP 423
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
65-492 4.71e-32

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


Pssm-ID: 410747 [Multi-domain]  Cd Length: 447  Bit Score: 127.73  E-value: 4.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGR-GTVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLAL---RDLG 139
Cdd:cd20654   1 GPIFTLRLGS-HPTLVVSSWEMAKECFTTNDKAFSSRpKTAAAKLMGYNYAMFGFAPyGPYWRELRKIATLELlsnRRLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 140 MGK----REGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRF-----SYEDKE---FQAVVRAAGg 207
Cdd:cd20654  80 KLKhvrvSEVDTSIKELYSLWSNNKKGGGGVLVEMKQWFADLTFNVILRMVVGKRYfggtaVEDDEEaerYKKAIREFM- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 208 TLLGVSSQGgQTYEMFSWFlrPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGP---ARDLVDAFLLKMAQEEQNPG 284
Cdd:cd20654 159 RLAGTFVVS-DAIPFLGWL--DFGGHEKAMKRTAKELDSILEEWLEEHRQKRSSSGKsknDEDDDDVMMLSILEDSQISG 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 --TEFTNKNMLMTVIyllFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:cd20654 236 ydADTVIKATCLELI---LGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLR 312
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFL--DADGRFRK-HEAFLPFSLGKRV 439
Cdd:cd20654 313 LYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLttHKDIDVRGqNFELIPFGSGRRS 392
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 13449277 440 CLGEGLAKAELFLFFTTILQAFSLESPcPPDTLSLKPTVsGLFNiPPAFQLQV 492
Cdd:cd20654 393 CPGVSFGLQVMHLTLARLLHGFDIKTP-SNEPVDMTEGP-GLTN-PKATPLEV 442
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
63-493 8.32e-32

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


Pssm-ID: 410693 [Multi-domain]  Cd Length: 438  Bit Score: 127.06  E-value: 8.32e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGPWRpvvVLVGQ-EAVREALggQAEE---FSGRGTVAMlegTFDGHGVFFSNGERWRQLRKFTMLALRDL 138
Cdd:cd11070   1 KLGAVKILFVSRWN---ILVTKpEYLTQIF--RRRDdfpKPGNQYKIP---AFYGPNVISSEGEDWKRYRKIVAPAFNER 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 139 GMGKREGEELIQAEARCLVETFQGTEGRPFDPSL--LLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVSSQG 216
Cdd:cd11070  73 NNALVWEESIRQAQRLIRYLLEEQPSAKGGGVDVrdLLQRLALNVIGEVGFGFDLPALDEEESSLHDTLNAIKLAIFPPL 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 217 GQTYEMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQnpgtEFTNKNMLMTV 296
Cdd:cd11070 153 FLNFPFLDRLPWVLFPSRKRAFKDVDEFLSELLDEVEAELSADSKGKQGTESVVASRLKRARRSG----GLTEKELLGNL 228
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 297 IYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRT--RLPYTDAVLHEAQRLLALVPmGIPRT 374
Cdd:cd11070 229 FIFFIAGHETTANTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEEDfpKLPYLLAVIYETLRLYPPVQ-LLNRK 307
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 375 LMRTTRF-----RGYTLPQGTEVFPLLGSILHDPNIFKH-PEEFNPDRFLD------ADGRFRKHE-AFLPFSLGKRVCL 441
Cdd:cd11070 308 TTEPVVVitglgQEIVIPKGTYVGYNAYATHRDPTIWGPdADEFDPERWGStsgeigAATRFTPARgAFIPFSAGPRACL 387
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
gi 13449277 442 GEGLAKAELFLFFTTILQAFSLESPcPPDTLSLKPtVSGLFNIPPAFQLQVR 493
Cdd:cd11070 388 GRKFALVEFVAALAELFRQYEWRVD-PEWEEGETP-AGATRDSPAKLRLRFR 437
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
64-468 8.51e-32

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


Pssm-ID: 410749 [Multi-domain]  Cd Length: 432  Bit Score: 126.83  E-value: 8.51e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPWRPVVVlVGQEAVREALGGQAEEFSGRGTVAMLEG-TFDGHGVFFSN-GERWRQLRKFTMLALRDLgmg 141
Cdd:cd20656   1 YGPIISVWIGSTLNVVV-SSSELAKEVLKEKDQQLADRHRTRSAARfSRNGQDLIWADyGPHYVKVRKLCTLELFTP--- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 KR-EGEELI-QAEARCLVETF------QGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYED-------KEFQAVVraAG 206
Cdd:cd20656  77 KRlESLRPIrEDEVTAMVESIfndcmsPENEGKPVVLRKYLSAVAFNNITRLAFGKRFVNAEgvmdeqgVEFKAIV--SN 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 207 GTLLGVSsqgGQTYEMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFL-LKmaqeEQNPGT 285
Cdd:cd20656 155 GLKLGAS---LTMAEHIPWLRWMFPLSEKAFAKHGARRDRLTKAIMEEHTLARQKSGGGQQHFVALLtLK----EQYDLS 227
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 286 EftnknmlMTVIYLLF----AGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQ 361
Cdd:cd20656 228 E-------DTVIGLLWdmitAGMDTTAISVEWAMAEMIRNPRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEAL 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 362 RLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHE-AFLPFSLGKRVC 440
Cdd:cd20656 301 RLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDIKGHDfRLLPFGAGRRVC 380
                       410       420
                ....*....|....*....|....*...
gi 13449277 441 LGEGLAKAELFLFFTTILQAFSLESPCP 468
Cdd:cd20656 381 PGAQLGINLVTLMLGHLLHHFSWTPPEG 408
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
62-478 1.51e-31

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: 125.76  E-value: 1.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  62 KKYGPVFTIYL-GpwRPVVVLVGQEAVREALGGQAEEFSGR--GTVAMLEGTfdgHGVFFSNGERWRQLRKFTM------ 132
Cdd:cd11043   3 KRYGPVFKTSLfG--RPTVVSADPEANRFILQNEGKLFVSWypKSVRKLLGK---SSLLTVSGEEHKRLRGLLLsflgpe 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 133 ------------LALRDLGMGKREGEELIQAEARCLveTFqgtegrpfdpslllaqatsNVVCSLLFGLrfsyEDKEFQA 200
Cdd:cd11043  78 alkdrllgdideLVRQHLDSWWRGKSVVVLELAKKM--TF-------------------ELICKLLLGI----DPEEVVE 132
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 201 VVRAAGGTLlgvssqggqTYEMFSWFLRpLPGP--HKqLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLlkmaQ 278
Cdd:cd11043 133 ELRKEFQAF---------LEGLLSFPLN-LPGTtfHR-ALKARKRIRKELKKIIEERRAELEKASPKGDLLDVLL----E 197
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 279 EEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTvgytLLLLMKY----PHVQKWVREE---LNRELGAGQAPSLGDRTRLP 351
Cdd:cd11043 198 EKDEDGDSLTDEEILDNILTLLFAGHETTSTT----LTLAVKFlaenPKVLQELLEEheeIAKRKEEGEGLTWEDYKSMK 273
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 352 YTDAVLHEAQRLLALVPmGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHeaFL 431
Cdd:cd11043 274 YTWQVINETLRLAPIVP-GVFRKALQDVEYKGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRWEGKGKGVPYT--FL 350
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*..
gi 13449277 432 PFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPcPPDTLSLKPTV 478
Cdd:cd11043 351 PFGGGPRLCPGAELAKLEILVFLHHLVTRFRWEVV-PDEKISRFPLP 396
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
64-464 3.34e-31

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: 125.07  E-value: 3.34e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRK-----FTMLALRDL 138
Cdd:cd11069   1 YGGLIRYRGLFGSERLLVTDPKALKHILVTNSYDFEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKilnpaFSYRHVKEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 139 -GMGKREGEELIQAEARcLVETfQGTEGRPFDPSLLLAQATSNVVCSLLFGLRF-SYEDKEfqAVVRAAGGTLLGvSSQG 216
Cdd:cd11069  81 yPIFWSKAEELVDKLEE-EIEE-SGDESISIDVLEWLSRATLDIIGLAGFGYDFdSLENPD--NELAEAYRRLFE-PTLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 217 GQTYEM-----FSWFLRPLPGPH-KQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDlVDAFLLKMAQEEQNPGTEFTNK 290
Cdd:cd11069 156 GSLLFIlllflPRWLVRILPWKAnREIRRAKDVLRRLAREIIREKKAALLEGKDDSG-KDILSILLRANDFADDERLSDE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 291 NML--MTVIylLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAG---QAPSLGDRTRLPYTDAVLHEAQRLLA 365
Cdd:cd11069 235 ELIdqILTF--LAAGHETTSTALTWALYLLAKHPDVQERLREEI-RAALPDppdGDLSYDDLDRLPYLNAVCRETLRLYP 311
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 366 LVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLDADGRFRKHEA-----FLPFSLGKRV 439
Cdd:cd11069 312 PVPL-TSREATKDTVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWLEPDGAASPGGAgsnyaLLTFLHGPRS 390
                       410       420
                ....*....|....*....|....*
gi 13449277 440 CLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:cd11069 391 CIGKKFALAEMKVLLAALVSRFEFE 415
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
113-479 5.31e-31

cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect cytochrome P450s from families 313 (CYP313) and 318 (CYP318), and similar proteins. These proteins may be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides. Their specific function is yet unknown. They belong to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410680 [Multi-domain]  Cd Length: 427  Bit Score: 124.25  E-value: 5.31e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 113 GHGVFFSNGERWRQLRK-----FTMLALRD-LGMGKREGEELIQaearcLVETFQGTEGrpFDPSLLLAQATSNVVCSLL 186
Cdd:cd11057  44 GRGLFSAPYPIWKLQRKalnpsFNPKILLSfLPIFNEEAQKLVQ-----RLDTYVGGGE--FDILPDLSRCTLEMICQTT 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 187 FGLRF---SYEDKEFQAVVRAaggtLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHHVSTLAAFT---VRQVQQHQGNLD 260
Cdd:cd11057 117 LGSDVndeSDGNEEYLESYER----LFELIAKRVLNPWLHPEFIYRLTGDYKEEQKARKILRAFSekiIEKKLQEVELES 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 261 ASGPARDLVDAF--------LLKMAQEEQnpgtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREEL 332
Cdd:cd11057 193 NLDSEEDEENGRkpqifidqLLELARNGE----EFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAMHPEVQEKVYEEI 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 333 NRELG-AGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRF-RGYTLPQGTevfPLLGSILH---DPNIF- 406
Cdd:cd11057 269 MEVFPdDGQFITYEDLQQLVYLEMVLKETMRLFPVGPL-VGRETTADIQLsNGVVIPKGT---TIVIDIFNmhrRKDIWg 344
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13449277 407 KHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVS 479
Cdd:cd11057 345 PDADQFDPDNFLPERSAQRHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYRLKTSLRLEDLRFKFNIT 417
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
75-466 5.48e-31

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: 124.29  E-value: 5.48e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  75 WRPVVVLVGQEAVREALGGQAEEFSgrgTVAMLEGT-FDGHGVFFSNGERWRQLRK-----FTMLALRD-LGMGKregeE 147
Cdd:cd20621  12 SKPLISLVDPEYIKEFLQNHHYYKK---KFGPLGIDrLFGKGLLFSEGEEWKKQRKllsnsFHFEKLKSrLPMIN----E 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 148 LIQaearclvETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRF---SYEDKEFQA--VVRAAGGTLLGVSSQGGQTYEM 222
Cdd:cd20621  85 ITK-------EKIKKLDNQNVNIIQFLQKITGEVVIRSFFGEEAkdlKINGKEIQVelVEILIESFLYRFSSPYFQLKRL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 223 F----SWFLRPLPGpHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIY 298
Cdd:cd20621 158 IfgrkSWKLFPTKK-EKKLQKRVKELRQFIEKIIQNRIKQIKKNKDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFIT 236
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 299 LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRT 378
Cdd:cd20621 237 FFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFLFPRVATQD 316
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 379 TRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTIL 458
Cdd:cd20621 317 HQIGDLKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWLNQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYIL 396

                ....*...
gi 13449277 459 QAFSLESP 466
Cdd:cd20621 397 KNFEIEII 404
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
57-476 6.12e-31

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


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 124.22  E-value: 6.12e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  57 LMRLSKKYGPVFTIYLGPWRPVVVlVGQEAVREALggQAEEFS---GRGTVAMLEGTfdGHGVF--FSNGERWRQ----- 126
Cdd:cd11068   5 LLRLADELGPIFKLTLPGRRVVVV-SSHDLIAELC--DESRFDkkvSGPLEELRDFA--GDGLFtaYTHEPNWGKahril 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 127 LRKFTMLALRDL-GMGKREGEELIQAEARclvetfQGTEGrPFDPSLLLAQATSNVVCSLLFGLRF-SYEDKEFQAVVRA 204
Cdd:cd11068  80 MPAFGPLAMRGYfPMMLDIAEQLVLKWER------LGPDE-PIDVPDDMTRLTLDTIALCGFGYRFnSFYRDEPHPFVEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 205 AGGTLLGVSSQGGqtyeMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNldASGPARDLVDAfLLKMAqeeqNPG 284
Cdd:cd11068 153 MVRALTEAGRRAN----RPPILNKLRRRAKRQFREDIALMRDLVDEIIAERRAN--PDGSPDDLLNL-MLNGK----DPE 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 T--EFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGaGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:cd11068 222 TgeKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAKARAEVDEVLG-DDPPPYEQVAKLRYIRRVLDETLR 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMgIPRTLMRTTRFRG-YTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLdaDGRFRKH--EAFLPFSLGKR 438
Cdd:cd11068 301 LWPTAPA-FARKPKEDTVLGGkYPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPERFL--PEEFRKLppNAWKPFGNGQR 377
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 13449277 439 VCLGEGLAKAELFLFFTTILQAFSLESpcPPD-------TLSLKP 476
Cdd:cd11068 378 ACIGRQFALQEATLVLAMLLQRFDFED--DPDyeldikeTLTLKP 420
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
65-461 1.47e-30

cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in flowering plants and could be classified into ten subfamilies, CYP93A-K. CYP93A appears to be the ancestor that was derived in flowering plants, and the remaining subfamiles show lineage-specific distribution: CYP93B and CYP93C are present in dicots; CYP93F is distributed only in Poaceae; CYP93G and CYP93J are monocot-specific; CYP93E is unique to legumes; CYP93H and CYP93K are only found in Aquilegia coerulea; and CYP93D is Brassicaceae-specific. Members of this family include: Glycyrrhiza echinata CYP93B1, also called licodione synthase (EC 1.14.14.140), that catalyzes the formation of licodione and 2-hydroxynaringenin from (2S)-liquiritigenin and (2S)-naringenin, respectively; and Glycine max CYP93A1, also called 3,9-dihydroxypterocarpan 6A-monooxygenase (EC 1.14.14.93), that is involved in the biosynthesis of the phytoalexin glyceollin. CYP93 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410748 [Multi-domain]  Cd Length: 433  Bit Score: 123.09  E-value: 1.47e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEG-TFDGHGVFFSN-GERWRQLRKFTMLALrdlgMGK 142
Cdd:cd20655   1 GPLLHLRIGS-VPCVVVSSASVAKEILKTHDLNFSSRPVPAAAESlLYGSSGFAFAPyGDYWKFMKKLCMTEL----LGP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REGEEL--IQAEArclVETF------QGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAV------VRAAGGT 208
Cdd:cd20655  76 RALERFrpIRAQE---LERFlrrlldKAEKGESVDIGKELMKLTNNIICRMIMGRSCSEENGEAEEVrklvkeSAELAGK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 209 LLGvssqggqtyEMFSWFLRPL--PGPHKQLLHHVSTLAAFTVRQVQQHQGNLDAS--GPARDLVDAfLLKMAQEEqnpG 284
Cdd:cd20655 153 FNA---------SDFIWPLKKLdlQGFGKRIMDVSNRFDELLERIIKEHEEKRKKRkeGGSKDLLDI-LLDAYEDE---N 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 TEF--TNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:cd20655 220 AEYkiTRNHIKAFILDLFIAGTDTSAATTEWAMAELINNPEVLEKAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLR 299
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFL------DADGRFRKHEAFLPFSLG 436
Cdd:cd20655 300 LHPPGPL-LVRESTEGCKINGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPERFLassrsgQELDVRGQHFKLLPFGSG 378
                       410       420
                ....*....|....*....|....*
gi 13449277 437 KRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd20655 379 RRGCPGASLAYQVVGTAIAAMVQCF 403
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
181-450 8.05e-30

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


Pssm-ID: 410682 [Multi-domain]  Cd Length: 422  Bit Score: 120.87  E-value: 8.05e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 181 VVCSLLFGLRFSYEDKEFQAVvRAAGGTLLGVSSQGGQTYEMFSWFLRPLPGPHKQLLHH-VSTLAAFTVRQVQQHQGNL 259
Cdd:cd11059 114 VVSHLLFGESFGTLLLGDKDS-RERELLRRLLASLAPWLRWLPRYLPLATSRLIIGIYFRaFDEIEEWALDLCARAESSL 192
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 260 DASGPARDLVdafLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNR-ELGA 338
Cdd:cd11059 193 AESSDSESLT---VLLLEKLKGLKKQGLDDLEIASEALDHIVAGHDTTAVTLTYLIWELSRPPNLQEKLREELAGlPGPF 269
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 339 GQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRT-TRFRGYTLPQGTEVfpllgSI----LH-DPNIFKHPEEF 412
Cdd:cd11059 270 RGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLPRVVPEGgATIGGYYIPGGTIV-----STqaysLHrDPEVFPDPEEF 344
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 13449277 413 NPDRFLDADG--RFRKHEAFLPFSLGKRVCLGEGLAKAEL 450
Cdd:cd11059 345 DPERWLDPSGetAREMKRAFWPFGSGSRMCIGMNLALMEM 384
PLN02966 PLN02966
cytochrome P450 83A1
61-474 3.55e-29

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 120.24  E-value: 3.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   61 SKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTvamlegtFDGHGvFFSNGERWRQLRKFT--MLALRDL 138
Cdd:PLN02966  59 AKKYGPILSYRIGS-RTMVVISSAELAKELLKTQDVNFADRPP-------HRGHE-FISYGRRDMALNHYTpyYREIRKM 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  139 GMGK-------REGEELIQAEARCLVETFQGTEGRP--FDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRaaggTL 209
Cdd:PLN02966 130 GMNHlfsptrvATFKHVREEEARRMMDKINKAADKSevVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFIK----IL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  210 LGVSSQGGQTYemFSWFLrplpgPHKQLLHHVSTLAAFTVRQVQQHQGNL-----DASGPAR------DLVDafLLKMAQ 278
Cdd:PLN02966 206 YGTQSVLGKIF--FSDFF-----PYCGFLDDLSGLTAYMKECFERQDTYIqevvnETLDPKRvkpeteSMID--LLMEIY 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  279 EEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAGQAPSL---GDRTRLPYTDA 355
Cdd:PLN02966 277 KEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEV-REYMKEKGSTFvteDDVKNLPYFRA 355
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  356 VLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLDADGRFRKHE-AFLPF 433
Cdd:PLN02966 356 LVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKGTDyEFIPF 435
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 13449277  434 SLGKRVCLGEGLAKAELFLFFTTILQAFSLESP--CPPDTLSL 474
Cdd:PLN02966 436 GSGRRMCPGMRLGAAMLEVPYANLLLNFNFKLPngMKPDDINM 478
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
111-475 6.13e-29

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: 118.46  E-value: 6.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 111 FD--GHGVFFSNGERWRQLRK-----FTMLALRDLgMgkregEELIQAEARCLVETFQG---TEGRPFDPSLLLAQATSN 180
Cdd:cd11064  44 FDllGDGIFNVDGELWKFQRKtasheFSSRALREF-M-----ESVVREKVEKLLVPLLDhaaESGKVVDLQDVLQRFTFD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 181 VVCSLLFG-----LRFSYEDKEF-QAVVRAAGGTLLGVSSQggqtyeMFSW-FLRPL-PGPHKQLLHHVSTLAAFT---V 249
Cdd:cd11064 118 VICKIAFGvdpgsLSPSLPEVPFaKAFDDASEAVAKRFIVP------PWLWkLKRWLnIGSEKKLREAIRVIDDFVyevI 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 250 RQVQQHQGNLDASGPAR-DLVDAFLLKMAQEEQNPGTEFtnknMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWV 328
Cdd:cd11064 192 SRRREELNSREEENNVReDLLSRFLASEEEEGEPVSDKF----LRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKI 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 329 REELNREL-----GAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTrfrgyTLPQGTEVFPllGSilhdp 403
Cdd:cd11064 268 REELKSKLpklttDESRVPTYEELKKLVYLHAALSESLRLYPPVPF-DSKEAVNDD-----VLPDGTFVKK--GT----- 334
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 404 NIFKHP--------------EEFNPDRFLDADGRFRKHEA--FLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE--- 464
Cdd:cd11064 335 RIVYSIyamgrmesiwgedaLEFKPERWLDEDGGLRPESPykFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKvvp 414
                       410
                ....*....|....*
gi 13449277 465 ----SPCPPDTLSLK 475
Cdd:cd11064 415 ghkvEPKMSLTLHMK 429
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
109-464 1.22e-28

cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium sporotrichioides cytochrome P450 58 (CYP58, also known as Tri4 and trichodiene oxygenase), and similar fungal proteins. CYP58 catalyzes the oxygenation of trichodiene during the biosynthesis of trichothecenes, which are sesquiterpenoid toxins that act by inhibiting protein biosynthesis. The CYP58-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410685 [Multi-domain]  Cd Length: 425  Bit Score: 117.74  E-value: 1.22e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 109 GTFDGHGVFFS--NGERWRQLRK-----FTMLALRDLgmgkregEELIQAEARCLV---ETFQGTeGRPFDPSLLLAQAT 178
Cdd:cd11062  38 GAFGAPGSTFStvDHDLHRLRRKalspfFSKRSILRL-------EPLIQEKVDKLVsrlREAKGT-GEPVNLDDAFRALT 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 179 SNVVCSLLFGLRFSY-EDKEFQAVVRAA--GGTLLGVSSQggqtyeMFSW---FLRPLPGPHKQLLHHVST----LAAFT 248
Cdd:cd11062 110 ADVITEYAFGRSYGYlDEPDFGPEFLDAlrALAEMIHLLR------HFPWllkLLRSLPESLLKRLNPGLAvfldFQESI 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 249 VRQVQQHQGNLDASGPARDLVDAFLLKMAQEeqNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWV 328
Cdd:cd11062 184 AKQVDEVLRQVSAGDPPSIVTSLFHALLNSD--LPPSEKTLERLADEAQTLIGAGTETTARTLSVATFHLLSNPEILERL 261
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 329 REELNRELGAGQA-PSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRT-LMRTTRFRGYTLPQGTEVfpllG----SILHD 402
Cdd:cd11062 262 REELKTAMPDPDSpPSLAELEKLPYLTAVIKEGLRLSYGVPTRLPRVvPDEGLYYKGWVIPPGTPV----SmssyFVHHD 337
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13449277 403 PNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:cd11062 338 EEIFPDPHEFRPERWLGAAEKGKLDRYLVPFSKGSRSCLGINLAYAELYLALAALFRRFDLE 399
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
57-466 2.48e-28

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 117.65  E-value: 2.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   57 LMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGR----GTVAMLEGTFDGhgVFFSNGERWRQLRKFTM 132
Cdd:PLN00110  56 LAKMAKRYGPVMFLKMGT-NSMVVASTPEAARAFLKTLDINFSNRppnaGATHLAYGAQDM--VFADYGPRWKLLRKLSN 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  133 LALrdLGMGKREGEELIQAEA-----RCLVETFQgtEGRPFDPSLLLAQATSNVVCSLLFGLRF----SYEDKEFQAVV- 202
Cdd:PLN00110 133 LHM--LGGKALEDWSQVRTVElghmlRAMLELSQ--RGEPVVVPEMLTFSMANMIGQVILSRRVfetkGSESNEFKDMVv 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  203 ---RAAGgtLLGVssqgGQTYEMFSWFlrPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFllkMAQE 279
Cdd:PLN00110 209 elmTTAG--YFNI----GDFIPSIAWM--DIQGIERGMKHLHKKFDKLLTRMIEEHTASAHERKGNPDFLDVV---MANQ 277
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  280 EQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHE 359
Cdd:PLN00110 278 ENSTGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRLVESDLPKLPYLQAICKE 357
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  360 AQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDA-----DGRFRKHEaFLPFS 434
Cdd:PLN00110 358 SFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEknakiDPRGNDFE-LIPFG 436
                        410       420       430
                 ....*....|....*....|....*....|..
gi 13449277  435 LGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN00110 437 AGRRICAGTRMGIVLVEYILGTLVHSFDWKLP 468
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
61-476 2.82e-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: 116.67  E-value: 2.82e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  61 SKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQaEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRK-----FTMLAL 135
Cdd:cd11052   8 IKQYGKNFLYWYGT-DPRLYVTEPELIKELLSKK-EGYFGKSPLQPGLKKLLGRGLVMSNGEKWAKHRRianpaFHGEKL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 136 RdlgmgkregeELIQAEARC---LVETFQ---GTEGRPFDPSLLLAQATSNVVCSLLFGLrfSYED--------KEFQAV 201
Cdd:cd11052  86 K----------GMVPAMVESvsdMLERWKkqmGEEGEEVDVFEEFKALTADIISRTAFGS--SYEEgkevfkllRELQKI 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 202 VRAAggtllgvssqggqTYEMFSWFLRPLPGPH----KQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMA 277
Cdd:cd11052 154 CAQA-------------NRDVGIPGSRFLPTKGnkkiKKLDKEIEDSLLEIIKKREDSLKMGRGDDYGDDLLGLLLEANQ 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 278 QEEQNPGTeftNKNMLM---TVIYllFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSlgDR-TRLPYT 353
Cdd:cd11052 221 SDDQNKNM---TVQEIVdecKTFF--FAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKDKPPS--DSlSKLKTV 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 354 DAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLDADGRFRKH-EAFL 431
Cdd:cd11052 294 SMVINESLRLYPPAVF-LTRKAKEDIKLGGLVIPKGTSIWIPVLALHHDEEIWgEDANEFNPERFADGVAKAAKHpMAFL 372
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 13449277 432 PFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE-SP----CPPDTLSLKP 476
Cdd:cd11052 373 PFGLGPRNCIGQNFATMEAKIVLAMILQRFSFTlSPtyrhAPTVVLTLRP 422
PLN02183 PLN02183
ferulate 5-hydroxylase
54-466 1.58e-27

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 115.72  E-value: 1.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   54 YSGLMRLSKKYGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGR-GTVAMLEGTFDGHGVFFSN-GERWRQLRKFT 131
Cdd:PLN02183  58 HRGLANLAKQYGGLFHMRMG-YLHMVAVSSPEVARQVLQVQDSVFSNRpANIAISYLTYDRADMAFAHyGPFWRQMRKLC 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  132 MLALrdLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGgTLLG 211
Cdd:PLN02183 137 VMKL--FSRKRAESWASVRDEVDSMVRSVSSNIGKPVNIGELIFTLTRNITYRAAFGSSSNEGQDEFIKILQEFS-KLFG 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  212 VSSQGgqtyEMFSWFLRPLP-GPHKQLLHHVSTLAAFT-------VRQVQQHQGNLDASGPARDLVDAFL-------LKM 276
Cdd:PLN02183 214 AFNVA----DFIPWLGWIDPqGLNKRLVKARKSLDGFIddiiddhIQKRKNQNADNDSEEAETDMVDDLLafyseeaKVN 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  277 AQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAV 356
Cdd:PLN02183 290 ESDDLQNSIKLTRDNIKAIIMDVMFGGTETVASAIEWAMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCT 369
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  357 LHEAQRLLALVPMGIPRTlMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADG-RFR-KHEAFLPFS 434
Cdd:PLN02183 370 LKETLRLHPPIPLLLHET-AEDAEVAGYFIPKRSRVMINAWAIGRDKNSWEDPDTFKPSRFLKPGVpDFKgSHFEFIPFG 448
                        410       420       430
                 ....*....|....*....|....*....|..
gi 13449277  435 LGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN02183 449 SGRRSCPGMQLGLYALDLAVAHLLHCFTWELP 480
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
66-474 1.33e-26

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: 111.78  E-value: 1.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  66 PVFTIYLGPWrPVVVLVGQEAVrEALGGQAEEFSGRGTVAMLEgTFDGHGVFFSNGERWRQLRK-------FTMLAlrdl 138
Cdd:cd20680  13 PLLKLWIGPV-PFVILYHAENV-EVILSSSKHIDKSYLYKFLH-PWLGTGLLTSTGEKWRSRRKmltptfhFTILS---- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 139 gmgkrEGEELIQAEARCLVETFQG-TEGRPFDPSLLLAQATSNVVCSLLFGLRF---SYEDKEF-QAVVRAaggtllgvs 213
Cdd:cd20680  86 -----DFLEVMNEQSNILVEKLEKhVDGEAFNCFFDITLCALDIICETAMGKKIgaqSNKDSEYvQAVYRM--------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 214 SQGGQTYEMFSWF----LRPLPGPHKQLLHHVSTLAAFT-------VRQVQQHQ---GNLDASGPARDLVDAFL--LKMA 277
Cdd:cd20680 152 SDIIQRRQKMPWLwldlWYLMFKEGKEHNKNLKILHTFTdnviaerAEEMKAEEdktGDSDGESPSKKKRKAFLdmLLSV 231
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 278 QEEQnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAP-SLGDRTRLPYTDAV 356
Cdd:cd20680 232 TDEE--GNKLSHEDIREEVDTFMFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSDRPvTMEDLKKLRYLECV 309
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 357 LHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLG 436
Cdd:cd20680 310 IKESLRLFPSVPL-FARSLCEDCEIRGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSGRHPYAYIPFSAG 388
                       410       420       430
                ....*....|....*....|....*....|....*...
gi 13449277 437 KRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSL 474
Cdd:cd20680 389 PRNCIGQRFALMEEKVVLSCILRHFWVEANQKREELGL 426
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
64-476 2.14e-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: 111.30  E-value: 2.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVA-MLEGTFdGHGVFFSNGERWRQLRKFTMLALRdlgmgK 142
Cdd:cd11046  10 YGPIYKLAFGP-KSFLVISDPAIAKHVLRSNAFSYDKKGLLAeILEPIM-GKGLIPADGEIWKKRRRALVPALH-----K 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REGEELIQAEARC---LVETFQ--GTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKE---FQAVVRAAggtllgVSS 214
Cdd:cd11046  83 DYLEMMVRVFGRCserLMEKLDaaAETGESVDMEEEFSSLTLDIIGLAVFNYDFGSVTEEspvIKAVYLPL------VEA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 215 QGGQTYEMFSW----FLRPLPGPHKQL--LH----HVSTLAAFTVRQVQQHQGNLdaSGPARDLVD-----AFLLKMAQE 279
Cdd:cd11046 157 EHRSVWEPPYWdipaALFIVPRQRKFLrdLKllndTLDDLIRKRKEMRQEEDIEL--QQEDYLNEDdpsllRFLVDMRDE 234
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 280 EqnpgteFTNKNM---LMTviyLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAV 356
Cdd:cd11046 235 D------VDSKQLrddLMT---MLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRV 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 357 LHEAQRLLALVPMGIPRTLMRTTRFRG-YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHE----AFL 431
Cdd:cd11046 306 LNESLRLYPQPPVLIRRAVEDDKLPGGgVKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEViddfAFL 385
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*
gi 13449277 432 PFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKP 476
Cdd:cd11046 386 PFGGGPRKCLGDQFALLEATVALAMLLRRFDFELDVGPRHVGMTT 430
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
63-476 4.14e-26

cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; Cytochrome p450 27B1 (CYP27B1) is also called calcidiol 1-monooxygenase (EC 1.14.15.18), 25-hydroxyvitamin D(3) 1-alpha-hydroxylase (VD3 1A hydroxylase), 25-hydroxyvitamin D-1 alpha hydroxylase, 25-OHD-1 alpha-hydroxylase, 25-hydroxycholecalciferol 1-hydroxylase, or 25-hydroxycholecalciferol 1-monooxygenase. It catalyzes the conversion of 25-hydroxyvitamin D3 (25(OH)D3) to 1-alpha,25-dihydroxyvitamin D3 (1,25(OH)2D3 or calcitriol), and of 24,25-dihydroxyvitamin D3 (24,25(OH)(2)D3) to 1-alpha,24,25-trihydroxyvitamin D3 (1alpha,24,25(OH)(3)D3). It is also active with 25-hydroxy-24-oxo-vitamin D3, and has an important role in normal bone growth, calcium metabolism, and tissue differentiation. CYP27B1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410741 [Multi-domain]  Cd Length: 430  Bit Score: 110.23  E-value: 4.14e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGPWRPVVV----LV-------GQEAVREALGGQAEEFSGRGtvamlegtfDGHGVFFSNGERWRQLRkfT 131
Cdd:cd20648   4 KYGPVWKASFGPILTVHVadpaLIeqvlrqeGKHPVRSDLSSWKDYRQLRG---------HAYGLLTAEGEEWQRLR--S 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 132 MLALRDLGMGKREG-EELIQAEARCLVETFQGTEGRPfDPSLLLAQATS------NVVCSLLFGLRFSYED----KEFQA 200
Cdd:cd20648  73 LLAKHMLKPKAVEAyAGVLNAVVTDLIRRLRRQRSRS-SPGVVKDIAGEfykfglEGISSVLFESRIGCLEanvpEETET 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 201 VVRAAGG----TLLgvssqggqTYEMFSWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLV-DAFLLK 275
Cdd:cd20648 152 FIQSINTmfvmTLL--------TMAMPKWLHRLFPKPWQRFCRSWDQMFAFAKGHIDRRMAEVAAKLPRGEAIeGKYLTY 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 276 MAQEEQNPgteftnknmlMTVIY-----LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRL 350
Cdd:cd20648 224 FLAREKLP----------MKSIYgnvteLLLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARM 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 351 PYTDAVLHEAQRLLALVPMG---IPRtlmRTTRFRGYTLPQGTevfplLGSILH-----DPNIFKHPEEFNPDRFLDADG 422
Cdd:cd20648 294 PLLKAVVKEVLRLYPVIPGNarvIPD---RDIQVGEYIIPKKT-----LITLCHyatsrDENQFPDPNSFRPERWLGKGD 365
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....
gi 13449277 423 RFRKHeAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLEsPCPPDTLsLKP 476
Cdd:cd20648 366 THHPY-ASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVR-PEPGGSP-VKP 416
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
116-474 5.29e-26

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


Pssm-ID: 410750 [Multi-domain]  Cd Length: 438  Bit Score: 110.20  E-value: 5.29e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 116 VFFSNGERWRQLRKFTML------ALRDLG-MGKREGEELIQAEARclvetfQGTEGRPFDPSLLLAQATSNVVCSL--- 185
Cdd:cd20657  53 VFAPYGPRWRLLRKLCNLhlfggkALEDWAhVRENEVGHMLKSMAE------ASRKGEPVVLGEMLNVCMANMLGRVmls 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 186 --LFGLRFSYEDKEFQAVV----RAAGgtLLGVssqgGQTYEMFSWF-LRPLPGPHKQLlhHvSTLAAFTVRQVQQHQGN 258
Cdd:cd20657 127 krVFAAKAGAKANEFKEMVvelmTVAG--VFNI----GDFIPSLAWMdLQGVEKKMKRL--H-KRFDALLTKILEEHKAT 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 259 LDASGPARDLVDAFLLkmAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGA 338
Cdd:cd20657 198 AQERKGKPDFLDFVLL--ENDDNGEGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGR 275
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 339 GQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFL 418
Cdd:cd20657 276 DRRLLESDIPNLPYLQAICKETFRLHPSTPLNLPRIASEACEVDGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFL 355
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13449277 419 -----DADGRFRKHEaFLPFSLGKRVCLGE--GLAKAELFLffTTILQAF--SLESPCPPDTLSL 474
Cdd:cd20657 356 pgrnaKVDVRGNDFE-LIPFGAGRRICAGTrmGIRMVEYIL--ATLVHSFdwKLPAGQTPEELNM 417
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
62-466 6.50e-26

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


Pssm-ID: 410697 [Multi-domain]  Cd Length: 434  Bit Score: 109.87  E-value: 6.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  62 KKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRgTVAMLEGTFDGHG---VFFSNGERWRQLRK------FTM 132
Cdd:cd11074   1 KKFGDIFLLRMGQ-RNLVVVSSPELAKEVLHTQGVEFGSR-TRNVVFDIFTGKGqdmVFTVYGEHWRKMRRimtvpfFTN 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 133 LALRDlgmgKREGEEliqAEARCLVETFQ-----GTEGRPFDPSLLLAQatSNVVCSLLFGLRFSYEDKEFQAVVRAagg 207
Cdd:cd11074  79 KVVQQ----YRYGWE---EEAARVVEDVKknpeaATEGIVIRRRLQLMM--YNNMYRIMFDRRFESEDDPLFVKLKA--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 208 tLLGVSSQGGQTYEM----FSWFLRPLPGPHKQLLHHV--STLAAFTVRQVQQHQgNLDASGPARDLVDAFLLKMAQEEQ 281
Cdd:cd11074 147 -LNGERSRLAQSFEYnygdFIPILRPFLRGYLKICKEVkeRRLQLFKDYFVDERK-KLGSTKSTKNEGLKCAIDHILDAQ 224
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 282 NPGtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQ 361
Cdd:cd11074 225 KKG-EINEDNVLYIVENINVAAIETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETL 303
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 362 RLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR-------FRkheaFLPFS 434
Cdd:cd11074 304 RLRMAIPLLVPHMNLHDAKLGGYDIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESKveangndFR----YLPFG 379
                       410       420       430
                ....*....|....*....|....*....|..
gi 13449277 435 LGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:cd11074 380 VGRRSCPGIILALPILGITIGRLVQNFELLPP 411
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
61-494 1.60e-25

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: 108.65  E-value: 1.60e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  61 SKKYGPVFTIYLGPwRPVVVLVGQEAVREaLGGQAEEFSGRGTVAM--LEGTFdGHGVFFSNGERWRQLRK-----FTML 133
Cdd:cd20640   8 RKQYGPIFTYSTGN-KQFLYVSRPEMVKE-INLCVSLDLGKPSYLKktLKPLF-GGGILTSNGPHWAHQRKiiapeFFLD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 134 ALRdlGMGKregeeLIQAEARCLVETFQ------GTEGRPFDPSLLLAQATSNVVCSLLFGLRFSyEDKEFQAVVRAagg 207
Cdd:cd20640  85 KVK--GMVD-----LMVDSAQPLLSSWEeridraGGMAADIVVDEDLRAFSADVISRACFGSSYS-KGKEIFSKLRE--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 208 tLLGVSSQGGQTYEMFSWFLRPLPGPHK--QLLHHVSTLAAFTVRQVQQhqgnldASGPARDLVDAfLLKMAQEEQNPGT 285
Cdd:cd20640 154 -LQKAVSKQSVLFSIPGLRHLPTKSNRKiwELEGEIRSLILEIVKEREE------ECDHEKDLLQA-ILEGARSSCDKKA 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 286 EFTN------KNmlmtvIYllFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAGQAPSLGDRTRLPYTDAVLHE 359
Cdd:cd20640 226 EAEDfivdncKN-----IY--FAGHETTAVTAAWCLMLLALHPEWQDRVRAEV-LEVCKGGPPDADSLSRMKTVTMVIQE 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 360 AQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLDADGRFRKH-EAFLPFSLGK 437
Cdd:cd20640 298 TLRLYPPAAF-VSREALRDMKLGGLVVPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSNGVAAACKPpHSYMPFGAGA 376
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 13449277 438 RVCLGEGLAKAELFLFFTTILQAFSlespcppdtLSLKPTvsglFNIPPAFQLQVRP 494
Cdd:cd20640 377 RTCLGQNFAMAELKVLVSLILSKFS---------FTLSPE----YQHSPAFRLIVEP 420
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
117-473 2.13e-25

cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins include: CYP78A5, which is expressed in leaf, flora and embryo, and has been reported to stimulate plant organ growth in Arabidopsis thaliana and to regulate plant architecture, ripening time, and fruit mass in tomato; Glycine max CYP78A10 that functions in regulating seed size/weight and pod number; and Physcomitrella patens CYP78A27 or CYP78A28, which together, are essential in bud formation. The CYP78 family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410699 [Multi-domain]  Cd Length: 426  Bit Score: 108.19  E-value: 2.13e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 117 FFSNGERWRQLRKFT---MLALRDLGMG----KREGEELIQAearclVETFQGTEGRPFDPSLLLAQATSNVVCSLlFGL 189
Cdd:cd11076  53 FAPYGEYWRNLRRIAsnhLFSPRRIAASepqrQAIAAQMVKA-----IAKEMERSGEVAVRKHLQRASLNNIMGSV-FGR 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 190 RFSYED-----KEFQAVVRAaGGTLLGvssqggqtyeMFSW-----FLRPLPgpHKQLLHHVSTLA----AFTVRQVQQH 255
Cdd:cd11076 127 RYDFEAgneeaEELGEMVRE-GYELLG----------AFNWsdhlpWLRWLD--LQGIRRRCSALVprvnTFVGKIIEEH 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 256 QGNLDASGPARDLVDAFLLKMAQEEQnpgteFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRE 335
Cdd:cd11076 194 RAKRSNRARDDEDDVDVLLSLQGEEK-----LSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAA 268
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 336 LGAGQAPSLGDRTRLPYTDAVLHEAQRLLalvPMGiP-----RTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPE 410
Cdd:cd11076 269 VGGSRRVADSDVAKLPYLQAVVKETLRLH---PPG-PllswaRLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPL 344
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 13449277 411 EFNPDRFLDADGR----FRKHEAFL-PFSLGKRVCLGEGLAKAELFLFFTTILQAFS-LESPCPPDTLS 473
Cdd:cd11076 345 EFKPERFVAAEGGadvsVLGSDLRLaPFGAGRRVCPGKALGLATVHLWVAQLLHEFEwLPDDAKPVDLS 413
PLN02687 PLN02687
flavonoid 3'-monooxygenase
60-466 2.59e-25

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 109.13  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   60 LSKKYGPVFTIYLGpWRPVVVLVGQEAVREALGGQAEEFSGR----GTVAMLEGTFDGhgVFFSNGERWRQLRK------ 129
Cdd:PLN02687  62 LAKTYGPLFRLRFG-FVDVVVAASASVAAQFLRTHDANFSNRppnsGAEHMAYNYQDL--VFAPYGPRWRALRKicavhl 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  130 FTMLALRDLgMGKREGEelIQAEARCLVETFQGTegrPFDPSLLLAQATSNVVCSLLFGLRF-----SYEDKEFQAVV-- 202
Cdd:PLN02687 139 FSAKALDDF-RHVREEE--VALLVRELARQHGTA---PVNLGQLVNVCTTNALGRAMVGRRVfagdgDEKAREFKEMVve 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  203 -RAAGGTLlgvssQGGQTYEMFSWF-LRPLPGPHKQLlhHvSTLAAFTVRQVQQHQ-GNLDASGPARDLVdAFLLKMAQE 279
Cdd:PLN02687 213 lMQLAGVF-----NVGDFVPALRWLdLQGVVGKMKRL--H-RRFDAMMNGIIEEHKaAGQTGSEEHKDLL-STLLALKRE 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  280 EQNPGTE--FTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVL 357
Cdd:PLN02687 284 QQADGEGgrITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVI 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  358 HEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFL------DADGRFRKHEaFL 431
Cdd:PLN02687 364 KETFRLHPSTPLSLPRMAAEECEINGYHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLpggehaGVDVKGSDFE-LI 442
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 13449277  432 PFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN02687 443 PFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELA 477
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
57-466 2.98e-25

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 108.76  E-value: 2.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   57 LMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGR-GTVAMLEGTFDGHGVFFSN-GERWRQLRKFTM-- 132
Cdd:PLN03112  57 LASLCKKYGPLVYLRLGS-VDAITTDDPELIREILLRQDDVFASRpRTLAAVHLAYGCGDVALAPlGPHWKRMRRICMeh 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  133 -LALRDLGMGKREGEEliqaEARCLVETF--QGTEGRPFDPSLLLAQATSNVVCSLLFGLRF-------SYEDKEFQAVV 202
Cdd:PLN03112 136 lLTTKRLESFAKHRAE----EARHLIQDVweAAQTGKPVNLREVLGAFSMNNVTRMLLGKQYfgaesagPKEAMEFMHIT 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  203 RAAGgTLLGVSSQGgqTYEMFsWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQ----GNLDASGPaRDLVDAfLLKMAQ 278
Cdd:PLN03112 212 HELF-RLLGVIYLG--DYLPA-WRWLDPYGCEKKMREVEKRVDEFHDKIIDEHRrarsGKLPGGKD-MDFVDV-LLSLPG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  279 EEQNPGTEftNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLH 358
Cdd:PLN03112 286 ENGKEHMD--DVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEELDSVVGRNRMVQESDLVHLNYLRCVVR 363
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  359 EAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR---------FRkhea 429
Cdd:PLN03112 364 ETFRMHPAGPFLIPHESLRATTINGYYIPAKTRVFINTHGLGRNTKIWDDVEEFRPERHWPAEGSrveishgpdFK---- 439
                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 13449277  430 FLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN03112 440 ILPFSAGKRKCPGAPLGVTMVLMALARLFHCFDWSPP 476
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
114-464 3.50e-25

cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed of fungal cytochrome P450s including: Aspergillus nidulans cytochrome P450 60B (CYP60B), also called versicolorin B desaturase, which catalyzes the conversion of versicolorin B to versicolorin A during sterigmatocystin biosynthesis; Fusarium sporotrichioides cytochrome P450 65A1 (CYP65A1), also called isotrichodermin C-15 hydroxylase, which catalyzes the hydroxylation at C-15 of isotricodermin in trichothecene biosynthesis; and Penicillium aethiopicum P450 monooxygenase vrtK, also called viridicatumtoxin synthesis protein K, which catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to produce viridicatumtoxin, a tetracycline-like fungal meroterpenoid. The CYP60B-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410681 [Multi-domain]  Cd Length: 419  Bit Score: 107.28  E-value: 3.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 114 HGVFFSNGERWRQLRK-----FTMLALRDLgmgkregEELIQAEARCLVETFQG--TEGRPFDPSLLLAQATSNVVCSLL 186
Cdd:cd11058  48 PSISTADDEDHARLRRllahaFSEKALREQ-------EPIIQRYVDLLVSRLREraGSGTPVDMVKWFNFTTFDIIGDLA 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 187 FGLRF-SYEDKEFQAVVRaaggTLLGVSSQGGQTYEM--FSWFLRPLPGPH-KQLLHHVSTLAAFTVRQVQQhqgNLDAS 262
Cdd:cd11058 121 FGESFgCLENGEYHPWVA----LIFDSIKALTIIQALrrYPWLLRLLRLLIpKSLRKKRKEHFQYTREKVDR---RLAKG 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 263 GPARDLVDAFLlkmaqEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAGQAP 342
Cdd:cd11058 194 TDRPDFMSYIL-----RNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEI-RSAFSSEDD 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 343 SLGDRT-RLPYTDAVLHEAQRLLALVPMGIPRtlmRTTRF----RGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRF 417
Cdd:cd11058 268 ITLDSLaQLPYLNAVIQEALRLYPPVPAGLPR---VVPAGgatiDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERW 344
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 13449277 418 L-DADGRFR--KHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:cd11058 345 LgDPRFEFDndKKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLE 394
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
65-461 2.30e-24

cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 (CYP81 or Cyp81) is CYP81E1, also called isoflavone 2'-hydroxylase, that catalyzes the hydroxylation of isoflavones, daidzein, and formononetin, to yield 2'-hydroxyisoflavones, 2'-hydroxydaidzein, and 2'-hydroxyformononetin, respectively. It is involved in the biosynthesis of isoflavonoid-derived antimicrobial compounds of legumes. CYP81 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 104.99  E-value: 2.30e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHG--VFFSNGERWRQLRKFTMLAL------- 135
Cdd:cd20653   1 GPIFSLRFGS-RLVVVVSSPSAAEECFTKNDIVLANRPRFLTGKHIGYNYTtvGSAPYGDHWRNLRRITTLEIfsshrln 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 136 RDLGMGKREGEELIQAEARCLVETFQGTEGRPfdpslLLAQATSNVVCSLLFGLRFSYED-------KEFQAVVRAagGT 208
Cdd:cd20653  80 SFSSIRRDEIRRLLKRLARDSKGGFAKVELKP-----LFSELTFNNIMRMVAGKRYYGEDvsdaeeaKLFRELVSE--IF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 209 LLGVSSQGGQTYEMFSWFlrplpgPHKQLLHHVSTLA----AFTVRQVQQHQGNLDASGpaRDLVDAFLlkmAQEEQNPG 284
Cdd:cd20653 153 ELSGAGNPADFLPILRWF------DFQGLEKRVKKLAkrrdAFLQGLIDEHRKNKESGK--NTMIDHLL---SLQESQPE 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 --TEFTNKNMLMTviyLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQR 362
Cdd:cd20653 222 yyTDEIIKGLILV---MLLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLR 298
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFldaDGRFRKHEAFLPFSLGKRVCLG 442
Cdd:cd20653 299 LYPAAPLLVPHESSEDCKIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERF---EGEEREGYKLIPFGLGRRACPG 375
                       410
                ....*....|....*....
gi 13449277 443 EGLAKAELFLFFTTILQAF 461
Cdd:cd20653 376 AGLAQRVVGLALGSLIQCF 394
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
147-493 1.06e-23

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


Pssm-ID: 410667 [Multi-domain]  Cd Length: 441  Bit Score: 103.53  E-value: 1.06e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 147 ELIQAEARCLVETFQG--TEGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVVRAAGGTLLGVssqggQTYEMFS 224
Cdd:cd11041  85 PDLQEELRAALDEELGscTEWTEVNLYDTVLRIVARVSARVFVGPPLCRNEEWLDLTINYTIDVFAAA-----AALRLFP 159
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 225 WFLRPLPGP----HKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLvdaFLLKMAQEEQNPGTEFTNKNMLMTVIYLL 300
Cdd:cd11041 160 PFLRPLVAPflpePRRLRRLLRRARPLIIPEIERRRKLKKGPKEDKPN---DLLQWLIEAAKGEGERTPYDLADRQLALS 236
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 301 FAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTR 380
Cdd:cd11041 237 FAAIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLVSLRRKVLKDVT 316
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 381 FR-GYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLD---ADGRFRKH------EAFLPFSLGKRVCLGEGLAKAEL 450
Cdd:cd11041 317 LSdGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYRlreQPGQEKKHqfvstsPDFLGFGHGRHACPGRFFASNEI 396
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 13449277 451 FLFFTTILQAFSLEspCPPDTLSLKPTVSGLFNIP-PAFQLQVR 493
Cdd:cd11041 397 KLILAHLLLNYDFK--LPEGGERPKNIWFGEFIMPdPNAKVLVR 438
PLN02655 PLN02655
ent-kaurene oxidase
57-442 2.13e-23

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 102.90  E-value: 2.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   57 LMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRG-TVAMLEGTFDGHGVFFSN-GERWRQLRKFTMLA 134
Cdd:PLN02655  25 FTKWSEIYGPIYTIRTGA-SSVVVLNSTEVAKEAMVTKFSSISTRKlSKALTVLTRDKSMVATSDyGDFHKMVKRYVMNN 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  135 LrdLGMGKregeeliQAEARCLVET---------FQGTEGRPFDP------------SLLLAQATSNVVCSLL---FGLR 190
Cdd:PLN02655 104 L--LGANA-------QKRFRDTRDMlienmlsglHALVKDDPHSPvnfrdvfenelfGLSLIQALGEDVESVYveeLGTE 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  191 FSYEDKeFQAVVRAAGGTLLGVSSQGGQTYemFSWFlrplpgPHKQLLHHVSTL----AAFTVRQVQQHQGNLdASGPAR 266
Cdd:PLN02655 175 ISKEEI-FDVLVHDMMMCAIEVDWRDFFPY--LSWI------PNKSFETRVQTTefrrTAVMKALIKQQKKRI-ARGEER 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  267 DLVDAFLLKMAqeeqnpgTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAGQAPSLGD 346
Cdd:PLN02655 245 DCYLDFLLSEA-------THLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLYREI-REVCGDERVTEED 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  347 RTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLdaDGRFRK 426
Cdd:PLN02655 317 LPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFL--GEKYES 394
                        410
                 ....*....|....*...
gi 13449277  427 HEAF--LPFSLGKRVCLG 442
Cdd:PLN02655 395 ADMYktMAFGAGKRVCAG 412
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
57-466 6.63e-23

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 101.69  E-value: 6.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   57 LMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRgtvAMLEG----TFDGHGVFFSN-GERWRQLRKFT 131
Cdd:PLN03234  54 LFRLSKLYGPIFTMKIGG-RRLAVISSAELAKELLKTQDLNFTAR---PLLKGqqtmSYQGRELGFGQyTAYYREMRKMC 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  132 MLAL---RDLGMGKREGEELIQaeaRCLVETFQGT-EGRPFDPSLLLAQATSNVVCSLLFGLRFSYEDKEFQAVV----- 202
Cdd:PLN03234 130 MVNLfspNRVASFRPVREEECQ---RMMDKIYKAAdQSGTVDLSELLLSFTNCVVCRQAFGKRYNEYGTEMKRFIdilye 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  203 -RAAGGTLLgvssqggqTYEMFSWF--LRPLPGPHKQLLHHVSTLAAFTVRQVQQhqgNLDASGPARDlVDAF--LLKMA 277
Cdd:PLN03234 207 tQALLGTLF--------FSDLFPYFgfLDNLTGLSARLKKAFKELDTYLQELLDE---TLDPNRPKQE-TESFidLLMQI 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  278 QEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVL 357
Cdd:PLN03234 275 YKDQPFSIKFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPNLPYLKAVI 354
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  358 HEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLD----ADGRFRKHEaFLP 432
Cdd:PLN03234 355 KESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMKehkgVDFKGQDFE-LLP 433
                        410       420       430
                 ....*....|....*....|....*....|....
gi 13449277  433 FSLGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN03234 434 FGSGRRMCPAMHLGIAMVEIPFANLLYKFDWSLP 467
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
66-485 7.49e-23

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


Pssm-ID: 410715 [Multi-domain]  Cd Length: 494  Bit Score: 101.22  E-value: 7.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  66 PVFTIYLGPWRPVVVLVGQeaVREA---LGGQAEEFSG-RGTVAMLEGTFDGHGVFFSNGERWRQLRKFtmlaLRDLgMG 141
Cdd:cd20622   2 PIIQLFIRPFGKPWVIVAD--FREAqdiLMRRTKEFDRsDFTIDVFGGIGPHHHLVKSTGPAFRKHRSL----VQDL-MT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 142 K------------REGEELI---QAEARClvetfqgTEGRPFDPSLLLAQATSNVVCSLLFG-------LRFSYE----- 194
Cdd:cd20622  75 PsflhnvaapaihSKFLDLIdlwEAKARL-------AKGRPFSAKEDIHHAALDAIWAFAFGinfdasqTRPQLElleae 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 195 --------------------DKEFQAVVRAAGgtllgvSSQGGQTYEM---FSWFLRPLPGPHKQLLHHVSTLAAFTVRQ 251
Cdd:cd20622 148 dstilpagldepvefpeaplPDELEAVLDLAD------SVEKSIKSPFpklSHWFYRNQPSYRRAAKIKDDFLQREIQAI 221
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 252 VQQHQGNLDaSGPARDLVDAFLL--KMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVR 329
Cdd:cd20622 222 ARSLERKGD-EGEVRSAVDHMVRreLAAAEKEGRKPDYYSQVIHDELFGYLIAGHDTTSTALSWGLKYLTANQDVQSKLR 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 330 EELNRELGAGQA----PSLGD--RTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLL--GSILH 401
Cdd:cd20622 301 KALYSAHPEAVAegrlPTAQEiaQARIPYLDAVIEEILRCANTAPI-LSREATVDTQVLGYSIPKGTNVFLLNngPSYLS 379
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 402 DP--------------NIFKHP-------EEFNPDRFLDADGRFRKHE------AFLPFSLGKRVCLGEGLAKAELFLFF 454
Cdd:cd20622 380 PPieidesrrssssaaKGKKAGvwdskdiADFDPERWLVTDEETGETVfdpsagPTLAFGLGPRGCFGRRLAYLEMRLII 459
                       490       500       510
                ....*....|....*....|....*....|.
gi 13449277 455 TTILQAFSLEsPCPPDtLSLKPTVSGLFNIP 485
Cdd:cd20622 460 TLLVWNFELL-PLPEA-LSGYEAIDGLTRMP 488
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
287-482 2.70e-22

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: 99.22  E-value: 2.70e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 287 FTNKNMLMTVIY-----LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQ 361
Cdd:cd20647 228 LVSKELTLEEIYanmteMLLAGVDTTSFTLSWATYLLARHPEVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETL 307
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 362 RLLALVPmGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFR-KHEAFLPFSLGKRVC 440
Cdd:cd20647 308 RLFPVLP-GNGRVTQDDLIVGGYLIPKGTQLALCHYSTSYDEENFPRAEEFRPERWLRKDALDRvDNFGSIPFGYGIRSC 386
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 13449277 441 LGEGLAKAELFLFFTTILQAFSLESpcPPDTLSLKPTVSGLF 482
Cdd:cd20647 387 IGRRIAELEIHLALIQLLQNFEIKV--SPQTTEVHAKTHGLL 426
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
57-461 4.15e-22

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: 98.16  E-value: 4.15e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  57 LMRLSKKYGPVF-TIYLGpwRPVVVLVGQEAVREALGGQAEEFS-GRGTVAMLEGTFDGhGVFFSNGERWRQLRK----- 129
Cdd:cd11045   3 ARQRYRRYGPVSwTGMLG--LRVVALLGPDANQLVLRNRDKAFSsKQGWDPVIGPFFHR-GLMLLDFDEHRAHRRimqqa 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 130 FTMLALRDLGMGKREG-EELIQAearclvetFQGTEGRPFDP---SLLLAQATSnvvcsLLFGLRFSYEDKEF------- 198
Cdd:cd11045  80 FTRSALAGYLDRMTPGiERALAR--------WPTGAGFQFYPaikELTLDLATR-----VFLGVDLGPEADKVnkafidt 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 199 ----QAVVRAA-GGTLLGVSSQGGQTYEMFswFLRPLPgphkqllhhvstlaaftvrqvQQHQGNLDasgparDLVDAfl 273
Cdd:cd11045 147 vrasTAIIRTPiPGTRWWRGLRGRRYLEEY--FRRRIP---------------------ERRAGGGD------DLFSA-- 195
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 274 lkMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNReLGAGQaPSLGDRTRLPYT 353
Cdd:cd11045 196 --LCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLA-LGKGT-LDYEDLGQLEVT 271
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 354 DAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHE-AFLP 432
Cdd:cd11045 272 DWVFKEALRLVPPVPT-LPRRAVKDTEVLGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAEDKVHRyAWAP 350
                       410       420
                ....*....|....*....|....*....
gi 13449277 433 FSLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd11045 351 FGGGAHKCIGLHFAGMEVKAILHQMLRRF 379
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
61-463 6.60e-22

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: 97.91  E-value: 6.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  61 SKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEgTFDGHGVFFSNGERWRQLRK-----FTMLAL 135
Cdd:cd20639   8 RKIYGKTFLYWFGP-TPRLTVADPELIREILLTRADHFDRYEAHPLVR-QLEGDGLVSLRGEKWAHHRRvitpaFHMENL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 136 RDL--GMGKREGEELIQAEARCLvetfQGTEGRpFDPSLLLAQATSNVVCSLLFGLrfSYEDKE--FQAVVRAAGGTLLG 211
Cdd:cd20639  86 KRLvpHVVKSVADMLDKWEAMAE----AGGEGE-VDVAEWFQNLTEDVISRTAFGS--SYEDGKavFRLQAQQMLLAAEA 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 212 VSSQGGQTYEMF-------SWFLrplpgpHKQLLHHVSTLaaFTVRQVQQHQGNLDASGpaRDLVDAFLLKMAQEEqnpG 284
Cdd:cd20639 159 FRKVYIPGYRFLptkknrkSWRL------DKEIRKSLLKL--IERRQTAADDEKDDEDS--KDLLGLMISAKNARN---G 225
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 TEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLL 364
Cdd:cd20639 226 EKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLY 305
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 365 AlvP-MGIPRTLMRTTRFRGYTLPQGTEV-FPLLgSILHDPNIF-KHPEEFNPDRFLDADGRFRKHE-AFLPFSLGKRVC 440
Cdd:cd20639 306 P--PaVATIRRAKKDVKLGGLDIPAGTELlIPIM-AIHHDAELWgNDAAEFNPARFADGVARAAKHPlAFIPFGLGPRTC 382
                       410       420
                ....*....|....*....|...
gi 13449277 441 LGEGLAKAELFLFFTTILQAFSL 463
Cdd:cd20639 383 VGQNLAILEAKLTLAVILQRFEF 405
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
299-450 7.85e-22

cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus nidulans cytochrome P450 59 (CYP59), also called sterigmatocystin biosynthesis P450 monooxygenase stcS, and similar fungal proteins. CYP59 is required for the conversion of versicolorin A to sterigmatocystin. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410674 [Multi-domain]  Cd Length: 403  Bit Score: 97.32  E-value: 7.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 299 LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSL-----GDRT--RLPYTDAVLHEAQRLL---ALVP 368
Cdd:cd11051 193 FLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAEHDEVFGPDPSAAAellreGPELlnQLPYTTAVIKETLRLFppaGTAR 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 369 MGIPRTLMRTTRFRGYTLPqGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR---FRKHeAFLPFSLGKRVCLGEGL 445
Cdd:cd11051 273 RGPPGVGLTDRDGKEYPTD-GCIVYVCHHAIHRDPEYWPRPDEFIPERWLVDEGHelyPPKS-AWRPFERGPRNCIGQEL 350

                ....*
gi 13449277 446 AKAEL 450
Cdd:cd11051 351 AMLEL 355
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
64-471 1.33e-21

fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This group includes Aspergillus nidulans phenylacetate 2-hydroxylase (encoded by the phacA gene) and similar fungal cytochrome P450s. PhacA catalyzes the ortho-hydroxylation of phenylacetate, the first step of A. nidulans phenylacetate catabolism. The PhacA-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410689 [Multi-domain]  Cd Length: 434  Bit Score: 97.00  E-value: 1.33e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAmlegTFdgHGVFFSN----------GERWRQLRKFTML 133
Cdd:cd11066   1 NGPVFQIRLGN-KRIVVVNSFASVRDLWIKNSSALNSRPTFY----TF--HKVVSSTqgftigtspwDESCKRRRKAAAS 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 134 AL------RDLGMGKREGEELIQaeaRCLVETFQGTEGrpFDPSLLLAQATSNVVCSLLFGLRF-SYEDKEFQAVVRAAG 206
Cdd:cd11066  74 ALnrpavqSYAPIIDLESKSFIR---ELLRDSAEGKGD--IDPLIYFQRFSLNLSLTLNYGIRLdCVDDDSLLLEIIEVE 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 207 GTLLGVSSQGGQtYEMFSWFLRPLPGPHK----------QLLHHVSTLAAFTVRQVQQhqgnldasGPARDLVDAFLLKm 276
Cdd:cd11066 149 SAISKFRSTSSN-LQDYIPILRYFPKMSKfreradeyrnRRDKYLKKLLAKLKEEIED--------GTDKPCIVGNILK- 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 277 aqeeqNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMK--YPHVQKWVREELNRELGAGQAP--SLGDRTRLPY 352
Cdd:cd11066 219 -----DKESKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHppGQEIQEKAYEEILEAYGNDEDAweDCAAEEKCPY 293
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 353 TDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLP 432
Cdd:cd11066 294 VVALVKETLRYFTVLPLGLPRKTTKDIVYNGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWLDASGDLIPGPPHFS 373
                       410       420       430       440
                ....*....|....*....|....*....|....*....|..
gi 13449277 433 FSLGKRVCLGEGLAKAELFLFFTTILQAFSL---ESPCPPDT 471
Cdd:cd11066 374 FGAGSRMCAGSHLANRELYTAICRLILLFRIgpkDEEEPMEL 415
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
70-450 1.81e-21

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: 95.45  E-value: 1.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  70 IYLGPWRPVVVLVGQEAVrEALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRK-FTMLALRDlgMGKREGEEL 148
Cdd:cd20629   3 FARREDRGVYVLLRHDDV-MAVLRDPRTFSSETYDATLGGPFLGHSILAMDGEEHRRRRRlLQPAFAPR--AVARWEEPI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 149 IQAEARCLVETFQGTEGrpFDpslLLAQATS----NVVCSLLfGLrfSYED-KEFQAVVraaggtllgvssqggqtYEMF 223
Cdd:cd20629  80 VRPIAEELVDDLADLGR--AD---LVEDFALelpaRVIYALL-GL--PEEDlPEFTRLA-----------------LAML 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 224 SWFLRPLPGPHKQLLHHVSTLAAFTVRQVQQHQGNldasgPARDLVDAFLLKMAQEEQNPGTEFTNKNMLmtviyLLFAG 303
Cdd:cd20629 135 RGLSDPPDPDVPAAEAAAAELYDYVLPLIAERRRA-----PGDDLISRLLRAEVEGEKLDDEEIISFLRL-----LLPAG 204
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVReelnrelgagqapslGDRTRLPytdAVLHEAQRLLALVPMgIPRTLMRTTRFRG 383
Cdd:cd20629 205 SDTTYRALANLLTLLLQHPEQLERVR---------------RDRSLIP---AAIEEGLRWEPPVAS-VPRMALRDVELDG 265
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 13449277 384 YTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDrfldadgrfRKHEAFLPFSLGKRVCLGEGLAKAEL 450
Cdd:cd20629 266 VTIPAGSLLDLSVGSANRDEDVYPDPDVFDID---------RKPKPHLVFGGGAHRCLGEHLARVEL 323
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
269-482 3.96e-21

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


Pssm-ID: 410743 [Multi-domain]  Cd Length: 426  Bit Score: 95.56  E-value: 3.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 269 VDaFLLKMAQEEQNPGTE----FTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSL 344
Cdd:cd20650 203 VD-FLQLMIDSQNSKETEshkaLSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLPNKAPPTY 281
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 345 GDRTRLPYTDAVLHEAQRLLAlVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRF 424
Cdd:cd20650 282 DTVMQMEYLDMVVNETLRLFP-IAGRLERVCKKDVEINGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDN 360
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 13449277 425 RKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLEsPCPPDTLSLKPTVSGLF 482
Cdd:cd20650 361 IDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFK-PCKETQIPLKLSLQGLL 417
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
265-476 1.54e-20

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: 93.96  E-value: 1.54e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 265 ARDLVDaflLKMA--QEEQNPGTE---------FTNKNMLMTVIY-----LLFAGTMTVSTTVGYTLLLLMKYPHVQKWV 328
Cdd:cd20646 194 GKKLID---KKMEeiEERVDRGEPvegeyltylLSSGKLSPKEVYgslteLLLAGVDTTSNTLSWALYHLARDPEIQERL 270
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 329 REELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTeVFPLLG-SILHDPNIFK 407
Cdd:cd20646 271 YQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYLFPKNT-LFHLCHyAVSHDETNFP 349
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 408 HPEEFNPDRFLDaDGRFRKHE-AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFslESPCPPDTLSLKP 476
Cdd:cd20646 350 EPERFKPERWLR-DGGLKHHPfGSIPFGYGVRACVGRRIAELEMYLALSRLIKRF--EVRPDPSGGEVKA 416
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
233-476 2.05e-20

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


Pssm-ID: 410771 [Multi-domain]  Cd Length: 436  Bit Score: 93.49  E-value: 2.05e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 233 PHKQLLHHVSTLA-AFTVRQVQ------QHQGNLDASGPAR--DLVDAFLLkmAQEEQnpGTEFTNKNMLMTVIYLLFAG 303
Cdd:cd20678 176 PHGRRFRRACQLAhQHTDKVIQqrkeqlQDEGELEKIKKKRhlDFLDILLF--AKDEN--GKSLSDEDLRAEVDTFMFEG 251
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 304 TMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVPmGIPRTLMR-TTRFR 382
Cdd:cd20678 252 HDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVP-GISRELSKpVTFPD 330
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 383 GYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFS 462
Cdd:cd20678 331 GRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSSKRHSHAFLPFSAGPRNCIGQQFAMNEMKVAVALTLLRFE 410
                       250
                ....*....|....*....
gi 13449277 463 LES-----PCPPDTLSLKP 476
Cdd:cd20678 411 LLPdptriPIPIPQLVLKS 429
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
261-453 3.00e-20

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: 92.69  E-value: 3.00e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 261 ASGPARDLVDAFLLKM------AQEEQNPG-TEFTNKNMLMTVIYLLFAG--TMTVSTTvgYTLLLLMKYPHVQKWVREE 331
Cdd:cd11082 183 AGEEPTCLLDFWTHEIleeikeAEEEGEPPpPHSSDEEIAGTLLDFLFASqdASTSSLV--WALQLLADHPDVLAKVREE 260
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 332 LNRELGAGQAPSLGDRTR-LPYTDAVLHEAQRLLALVPMgIPrtlMRTTR-FR---GYTLPQGTEVFPLLGSILHDPniF 406
Cdd:cd11082 261 QARLRPNDEPPLTLDLLEeMKYTRQVVKEVLRYRPPAPM-VP---HIAKKdFPlteDYTVPKGTIVIPSIYDSCFQG--F 334
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 13449277 407 KHPEEFNPDRFLD---ADGRFRKHeaFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd11082 335 PEPDKFDPDRFSPerqEDRKYKKN--FLVFGAGPHQCVGQEYAINHLMLF 382
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
64-476 1.08e-19

cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 clan, which is generally associated with the metabolism of a diversity of fairly hydrophobic compounds including fatty acids and isoprenoids, with the catabolism of hormones (brassinosteroids and gibberellin, GA) and with the biosynthesis of cytokinins. Arabidopsis thaliana CYP709B3 is involved in abscisic acid (ABA) and salt stress response. CYP709 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410734 [Multi-domain]  Cd Length: 431  Bit Score: 91.36  E-value: 1.08e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFdGHGVFFSNGERWRQLRK-----FTMLALRdl 138
Cdd:cd20641  11 YGETFLYWQGT-TPRICISDHELAKQVLSDKFGFFGKSKARPEILKLS-GKGLVFVNGDDWVRHRRvlnpaFSMDKLK-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 139 gmgkregeELIQAEARCLVETFQG---------TEGRPFDPSLLLAQATSNVVCSLLFGLrfSYED--------KEFQAV 201
Cdd:cd20641  87 --------SMTQVMADCTERMFQEwrkqrnnseTERIEVEVSREFQDLTADIIATTAFGS--SYAEgievflsqLELQKC 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 202 VRAAggtLLGVSSQGGQTyemfswflrpLPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPARDLVDAFLLKMAQEEQ 281
Cdd:cd20641 157 AAAS---LTNLYIPGTQY----------LPTPRNLRVWKLEKKVRNSIKRIIDSRLTSEGKGYGDDLLGLMLEAASSNEG 223
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 282 NPGTEftnKNMLMTVIY-----LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAV 356
Cdd:cd20641 224 GRRTE---RKMSIDEIIdecktFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMV 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 357 LHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEV-FPLLgsILH-DPNIF-KHPEEFNPDRFLDADGRFRKH-EAFLP 432
Cdd:cd20641 301 LMETLRLYGPVIN-IARRASEDMKLGGLEIPKGTTIiIPIA--KLHrDKEVWgSDADEFNPLRFANGVSRAATHpNALLS 377
                       410       420       430       440
                ....*....|....*....|....*....|....*....|....*....
gi 13449277 433 FSLGKRVCLGEGLAKAELFLFFTTILQAFSLE-SP----CPPDTLSLKP 476
Cdd:cd20641 378 FSLGPRACIGQNFAMIEAKTVLAMILQRFSFSlSPeyvhAPADHLTLQP 426
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
295-464 4.19e-19

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


Pssm-ID: 410736 [Multi-domain]  Cd Length: 425  Bit Score: 89.39  E-value: 4.19e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 295 TVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnreLGAGQApSLGDRTRL----PYTDAVLHEAQRLLAlVPMG 370
Cdd:cd20643 238 SVTELMAGGVDTTSMTLQWTLYELARNPNVQEMLRAEV---LAARQE-AQGDMVKMlksvPLLKAAIKETLRLHP-VAVS 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 371 IPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHeafLPFSLGKRVCLGEGLAKAEL 450
Cdd:cd20643 313 LQRYITEDLVLQNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN---LGFGFGPRQCLGRRIAETEM 389
                       170
                ....*....|....
gi 13449277 451 FLFFTTILQAFSLE 464
Cdd:cd20643 390 QLFLIHMLENFKIE 403
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
265-465 1.25e-18

cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; Cytochrome P450 24A1 (CYP24A1, EC 1.14.15.16) is also called 1,25-dihydroxyvitamin D(3) 24-hydroxylase (24-OHase), vitamin D(3) 24-hydroxylase, or cytochrome P450-CC24. It catalyzes the NADPH-dependent 24-hydroxylation of calcidiol (25-hydroxyvitamin D(3)) and calcitriol (1-alpha,25-dihydroxyvitamin D(3) or 1,25(OH)2D3). CYP24A1 regulates vitamin D activity through its hydroxylation of calcitriol, the physiologically active vitamin D hormone, which controls gene-expression and signal-transduction processes associated with calcium homeostasis, cellular growth, and the maintenance of heart, muscle, immune, and skin function. CYP24A1 belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410738 [Multi-domain]  Cd Length: 419  Bit Score: 87.94  E-value: 1.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 265 ARDLVDAFLLKMAQEEQNP-------GTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELG 337
Cdd:cd20645 193 AKHCIDKRLQRYSQGPANDflcdiyhDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQKLLQEIQSVLP 272
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 338 AGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEV---FPLLGSilhDPNIFKHPEEFNP 414
Cdd:cd20645 273 ANQTPRAEDLKNMPYLKACLKESMRLTPSVPF-TSRTLDKDTVLGDYLLPKGTVLminSQALGS---SEEYFEDGRQFKP 348
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 13449277 415 DRFLDadgrfRKHE----AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLES 465
Cdd:cd20645 349 ERWLQ-----EKHSinpfAHVPFGIGKRMCIGRRLAELQLQLALCWIIQKYQIVA 398
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
289-476 1.26e-18

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


Pssm-ID: 410735 [Multi-domain]  Cd Length: 431  Bit Score: 88.11  E-value: 1.26e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 289 NKNMLMT---VI------YllFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGaGQAPSLGDRTRLPYTDAVLHE 359
Cdd:cd20642 225 NKNGGMStedVIeecklfY--FAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFG-NNKPDFEGLNHLKVVTMILYE 301
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 360 AQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVF-PLLgSILHDPNIF-KHPEEFNPDRFldADG---RFRKHEAFLPFS 434
Cdd:cd20642 302 VLRLYPPVIQ-LTRAIHKDTKLGDLTLPAGVQVSlPIL-LVHRDPELWgDDAKEFNPERF--AEGiskATKGQVSYFPFG 377
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13449277 435 LGKRVCLGEGLAKAELFLFFTTILQAFSLE-SP----CPPDTLSLKP 476
Cdd:cd20642 378 WGPRICIGQNFALLEAKMALALILQRFSFElSPsyvhAPYTVLTLQP 424
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
63-468 1.30e-18

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: 88.36  E-value: 1.30e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  63 KYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRgTVAMLEGTFDGHGVFFSNGERWRQLRKFTMLALRDLGMgk 142
Cdd:cd20649   1 KYGPICGYYIGR-RMFVVIAEPDMIKQVLVKDFNNFTNR-MKANLITKPMSDSLLCLRDERWKRVRSILTPAFSAAKM-- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 143 REGEELIQAEARCLVETFQ--GTEGRPFDPSLLLAQATSNVVCSLLFGLR----------FSYEDKEFQAVVRAAGGTLL 210
Cdd:cd20649  77 KEMVPLINQACDVLLRNLKsyAESGNAFNIQRCYGCFTMDVVASVAFGTQvdsqknpddpFVKNCKRFFEFSFFRPILIL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 211 GVSsqggqtyemFSWFLRPLPG--PHKQLlHHVSTLAAFTVRQVQQHQGNLDASGPARDLV------------------- 269
Cdd:cd20649 157 FLA---------FPFIMIPLARilPNKSR-DELNSFFTQCIRNMIAFRDQQSPEERRRDFLqlmldartsakflsvehfd 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 270 ---DAFLLKMAQEEQNPGTE----------FTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNREL 336
Cdd:cd20649 227 ivnDADESAYDGHPNSPANEqtkpskqkrmLTEDEIVGQAFIFLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFF 306
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 337 GAGQAPSLGDRTRLPYTDAVLHEAQRLLALVpMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDR 416
Cdd:cd20649 307 SKHEMVDYANVQELPYLDMVIAETLRMYPPA-FRFAREAAEDCVVLGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPER 385
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|...
gi 13449277 417 FlDADGRFRKHE-AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESpCP 468
Cdd:cd20649 386 F-TAEAKQRRHPfVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQA-CP 436
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
62-450 1.44e-18

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 87.97  E-value: 1.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  62 KKYGPVF-TIYLGpwRPVVVLVGQEAVREALGGQAEEFSGR--GTVAMLEGTfdgHGVFFSNGERWRQLRKftMLAlRDL 138
Cdd:cd20636  20 EKYGNVFkTHLLG--RPVIRVTGAENIRKILLGEHTLVSTQwpQSTRILLGS---NTLLNSVGELHRQRRK--VLA-RVF 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 139 GMGKREG-----EELIQAEAR--ClvetfqgTEGRPFDPSLLLAQATSNVVCSLLFGLRFsyEDKEFQAVVRaaggtllg 211
Cdd:cd20636  92 SRAALESylpriQDVVRSEVRgwC-------RGPGPVAVYTAAKSLTFRIAVRILLGLRL--EEQQFTYLAK-------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 212 vssqggqTYE--MFSWFLRPLPGPHKQLLHHV---STLAAFTVRQVQQ--HQGNLDASGPARDlvdaFLLKMAQEEqnpG 284
Cdd:cd20636 155 -------TFEqlVENLFSLPLDVPFSGLRKGIkarDILHEYMEKAIEEklQRQQAAEYCDALD----YMIHSAREN---G 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 TEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREEL-NRELGAG-----QAPSLGDRTRLPYTDAVLH 358
Cdd:cd20636 221 KELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELvSHGLIDQcqccpGALSLEKLSRLRYLDCVVK 300
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 359 EAQRLLALVPMGIpRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRF-----LDADGRFRkheaFLPF 433
Cdd:cd20636 301 EVLRLLPPVSGGY-RTALQTFELDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFgvereESKSGRFN----YIPF 375
                       410
                ....*....|....*..
gi 13449277 434 SLGKRVCLGEGLAKAEL 450
Cdd:cd20636 376 GGGVRSCIGKELAQVIL 392
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
284-477 3.81e-18

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 86.96  E-value: 3.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  284 GTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREE---LNRELGAGQAPSLGDRTRLPYTDAVLHEA 360
Cdd:PLN02987 260 DDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEhekIRAMKSDSYSLEWSDYKSMPFTQCVVNET 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  361 QRLLALVPmGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVC 440
Cdd:PLN02987 340 LRVANIIG-GIFRRAMTDIEVKGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQSNSGTTVPSNVFTPFGGGPRLC 418
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 13449277  441 LGEGLAKAELFLFFTTILQAFSLeSPCPPDTLSLKPT 477
Cdd:PLN02987 419 PGYELARVALSVFLHRLVTRFSW-VPAEQDKLVFFPT 454
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
270-488 4.74e-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 [Multi-domain]  Cd Length: 432  Bit Score: 86.41  E-value: 4.74e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 270 DAFLLKMAQEEQNpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDR-- 347
Cdd:cd20638 210 DALQLLIEHSRRN-GEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEKGLLSTKPNENKEls 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 348 ----TRLPYTDAVLHEAQRLLALVPMGIpRTLMRTTRFRGYTLPQGTEVfplLGSI--LHD-PNIFKHPEEFNPDRFLDA 420
Cdd:cd20638 289 mevlEQLKYTGCVIKETLRLSPPVPGGF-RVALKTFELNGYQIPKGWNV---IYSIcdTHDvADIFPNKDEFNPDRFMSP 364
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 13449277 421 DGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSGLFNIPPAF 488
Cdd:cd20638 365 LPEDSSRFSFIPFGGGSRSCVGKEFAKVLLKIFTVELARHCDWQLLNGPPTMKTSPTVYPVDNLPAKF 432
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
64-462 1.52e-17

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: 84.53  E-value: 1.52e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  64 YGPVFTIYLgPWRPVVVLVGQEAVREALGGQAEEFSGRGTVAMLEGTFDGHGVFFSNGERWRQLRkfTMLA-------LR 136
Cdd:cd11063   1 YGNTFEVNL-LGTRVIFTIEPENIKAVLATQFKDFGLGERRRDAFKPLLGDGIFTSDGEEWKHSR--ALLRpqfsrdqIS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 137 DLGMGKREGEELIQAEARClvetfqgteGRPFDPSLLLAQATSNVVCSLLFG-----LRFSYEDKEFQAVVRA--AGGTL 209
Cdd:cd11063  78 DLELFERHVQNLIKLLPRD---------GSTVDLQDLFFRLTLDSATEFLFGesvdsLKPGGDSPPAARFAEAfdYAQKY 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 210 LGVSSQGGQtyemFSWFLRplpgpHKQLLHHVSTLAAFTVRQVQQ----HQGNLDASGPARDLvdaFLLKMAQEEQNPGT 285
Cdd:cd11063 149 LAKRLRLGK----LLWLLR-----DKKFREACKVVHRFVDPYVDKalarKEESKDEESSDRYV---FLDELAKETRDPKE 216
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 286 EftnKNMLMTViylLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLA 365
Cdd:cd11063 217 L---RDQLLNI---LLAGRDTTASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYP 290
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 366 LVPMGIpRTLMRTTrfrgyTLP--------------QGTEV-FPLLGsiLH-DPNIF-KHPEEFNPDRFLDADgrfRKHE 428
Cdd:cd11063 291 PVPLNS-RVAVRDT-----TLPrgggpdgkspifvpKGTRVlYSVYA--MHrRKDIWgPDAEEFRPERWEDLK---RPGW 359
                       410       420       430
                ....*....|....*....|....*....|....
gi 13449277 429 AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFS 462
Cdd:cd11063 360 EYLPFNGGPRICLGQQFALTEASYVLVRLLQTFD 393
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
62-450 4.52e-17

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 83.45  E-value: 4.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   62 KKYGPVF-TIYLGPwrPVVVLVGQEAVREALGGQAEEFsgRGTV-AMLEGTFDGHGVFFSNGERWRQLRKFTMLALrdLG 139
Cdd:PLN02196  66 KRYGSVFkTHVLGC--PCVMISSPEAAKFVLVTKSHLF--KPTFpASKERMLGKQAIFFHQGDYHAKLRKLVLRAF--MP 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  140 MGKREGEELIQAEARclvETFQGTEGRPFDPSLLLAQATSNVVCSLLFGL-RFSY-EDKEFQAVVRAAGGTLLGVSsqgg 217
Cdd:PLN02196 140 DAIRNMVPDIESIAQ---ESLNSWEGTQINTYQEMKTYTFNVALLSIFGKdEVLYrEDLKRCYYILEKGYNSMPIN---- 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  218 qtyemfswflrpLPGPhkqlLHHVSTLAAFTVRQV------QQHQGNLDASgparDLVDAFllkMAQEEqnpgtEFTNKN 291
Cdd:PLN02196 213 ------------LPGT----LFHKSMKARKELAQIlakilsKRRQNGSSHN----DLLGSF---MGDKE-----GLTDEQ 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  292 MLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREE---LNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLLALVP 368
Cdd:PLN02196 265 IADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEqmaIRKDKEEGESLTWEDTKKMPLTSRVIQETLRVASILS 344
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  369 MGIpRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADgrfrKHEAFLPFSLGKRVCLGEGLAKA 448
Cdd:PLN02196 345 FTF-REAVEDVEYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFEVAP----KPNTFMPFGNGTHSCPGNELAKL 419

                 ..
gi 13449277  449 EL 450
Cdd:PLN02196 420 EI 421
PLN02500 PLN02500
cytochrome P450 90B1
230-464 8.20e-17

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 82.99  E-value: 8.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  230 LPG-PHKQLLHHVSTLAAFTVRQVQQHQGNLdaSGPARDLVDAFLLKMAQEEQNPGTEftnkNMLMTVIYLLFAGTMTVS 308
Cdd:PLN02500 223 FPGtAYRKALKSRATILKFIERKMEERIEKL--KEEDESVEEDDLLGWVLKHSNLSTE----QILDLILSLLFAGHETSS 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  309 TTVGYTLLLLMKYPHVQKWVREE------LNRELGAGQApSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFR 382
Cdd:PLN02500 297 VAIALAIFFLQGCPKAVQELREEhleiarAKKQSGESEL-NWEDYKKMEFTQCVINETLRLGNVVRF-LHRKALKDVRYK 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  383 GYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGR-------FRKHEAFLPFSLGKRVCLGEGLAKAELFLFFT 455
Cdd:PLN02500 375 GYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRggssgssSATTNNFMPFGGGPRLCAGSELAKLEMAVFIH 454

                 ....*....
gi 13449277  456 TILQAFSLE 464
Cdd:PLN02500 455 HLVLNFNWE 463
PLN02936 PLN02936
epsilon-ring hydroxylase
51-464 2.79e-16

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 81.38  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   51 GALYSGLMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSgRGTVAMLEGTFDGHGVFFSNGERWRQLRKF 130
Cdd:PLN02936  36 GALFLPLFKWMNEYGPVYRLAAGP-RNFVVVSDPAIAKHVLRNYGSKYA-KGLVAEVSEFLFGSGFAIAEGELWTARRRA 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  131 TMLALRdlgmgKREGEELIQaeaRC-------LVETFQGT--EGRPFDPSLLLAQATSNVVcsllfGLR-FSYEdkeFQA 200
Cdd:PLN02936 114 VVPSLH-----RRYLSVMVD---RVfckcaerLVEKLEPValSGEAVNMEAKFSQLTLDVI-----GLSvFNYN---FDS 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  201 VVRAAggTLLGVSSQGGQTYEMFSWFLrpLPGPHKQLLHHVSTlaaftvRQVQQHqgnlDASGPARDLVDAFLLKM---- 276
Cdd:PLN02936 178 LTTDS--PVIQAVYTALKEAETRSTDL--LPYWKVDFLCKISP------RQIKAE----KAVTVIRETVEDLVDKCkeiv 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  277 -AQEEQNPGTEFTNKNMLMTVIYL-------------------LFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNREL 336
Cdd:PLN02936 244 eAEGEVIEGEEYVNDSDPSVLRFLlasreevssvqlrddllsmLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVL 323
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  337 GaGQAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDR 416
Cdd:PLN02936 324 Q-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPER 402
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 13449277  417 FlDADG--------RFRkheaFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:PLN02936 403 F-DLDGpvpnetntDFR----YIPFSGGPRKCVGDQFALLEAIVALAVLLQRLDLE 453
PLN02302 PLN02302
ent-kaurenoic acid oxidase
256-464 4.26e-16

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 80.53  E-value: 4.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  256 QGNLDASGPARDLVDAFllkMAQEEQNpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREElnRE 335
Cdd:PLN02302 256 SRKQNISPRKKDMLDLL---LDAEDEN-GRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAE--QE 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  336 LGAGQAP------SLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHP 409
Cdd:PLN02302 330 EIAKKRPpgqkglTLKDVRKMEYLSQVIDETLRLINISLT-VFREAKTDVEVNGYTIPKGWKVLAWFRQVHMDPEVYPNP 408
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 13449277  410 EEFNPDRFldaDGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:PLN02302 409 KEFDPSRW---DNYTPKAGTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLE 460
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
299-486 5.84e-16

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


Pssm-ID: 410666 [Multi-domain]  Cd Length: 432  Bit Score: 79.72  E-value: 5.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 299 LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAP-----SLGDRTRLPYTDAVLHEAQRLLAlvPMGIPR 373
Cdd:cd11040 231 LLWAINANTIPAAFWLLAHILSDPELLERIREEIEPAVTPDSGTnaildLTDLLTSCPLLDSTYLETLRLHS--SSTSVR 308
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 374 TLMR-TTRFRGYTLPQGTEVFpLLGSILH-DPNIF-KHPEEFNPDRFLDADG---RFRKHEAFLPFSLGKRVCLGEGLAK 447
Cdd:cd11040 309 LVTEdTVLGGGYLLRKGSLVM-IPPRLLHmDPEIWgPDPEEFDPERFLKKDGdkkGRGLPGAFRPFGGGASLCPGRHFAK 387
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 13449277 448 AELFLFFTTILQAFSLESPCPPDTLSLKPTVSGLFNIPP 486
Cdd:cd11040 388 NEILAFVALLLSRFDVEPVGGGDWKVPGMDESPGLGILP 426
PLN02738 PLN02738
carotene beta-ring hydroxylase
284-449 1.86e-15

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 79.19  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  284 GTEFTNKNM---LMTviyLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGqAPSLGDRTRLPYTDAVLHEA 360
Cdd:PLN02738 384 GDDVSSKQLrddLMT---MLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDR-FPTIEDMKKLKYTTRVINES 459
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  361 QRLLALVPMGIPRTLmRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRF-LDADGRFRKHEAF--LPFSLGK 437
Cdd:PLN02738 460 LRLYPQPPVLIRRSL-ENDMLGGYPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWpLDGPNPNETNQNFsyLPFGGGP 538
                        170
                 ....*....|..
gi 13449277  438 RVCLGEGLAKAE 449
Cdd:PLN02738 539 RKCVGDMFASFE 550
PLN02290 PLN02290
cytokinin trans-hydroxylase
261-476 3.69e-15

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 77.93  E-value: 3.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  261 ASGPARDLVDAFLLKMaqeEQNPGTEFT-NKNMLM-TVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGa 338
Cdd:PLN02290 287 SSSYGDDLLGMLLNEM---EKKRSNGFNlNLQLIMdECKTFFFAGHETTALLLTWTLMLLASNPTWQDKVRAEVAEVCG- 362
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  339 GQAPSLGDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVF-PLLgSILHDPNIF-KHPEEFNPDR 416
Cdd:PLN02290 363 GETPSVDHLSKLTLLNMVINESLRLYPPATL-LPRMAFEDIKLGDLHIPKGLSIWiPVL-AIHHSEELWgKDANEFNPDR 440
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13449277  417 FldADGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE-----SPCPPDTLSLKP 476
Cdd:PLN02290 441 F--AGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTisdnyRHAPVVVLTIKP 503
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
262-452 4.00e-15

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


Pssm-ID: 410730 [Multi-domain]  Cd Length: 430  Bit Score: 77.20  E-value: 4.00e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 262 SGPARDLVDAF--LLKMAQEEqnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREEL--NRELG 337
Cdd:cd20637 198 GTQGKDYADALdiLIESAKEH---GKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLREELrsNGILH 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 338 AG----QAPSLGDRTRLPYTDAVLHEAQRLLALVPMGIpRTLMRTTRFRGYTLPQGTEVfplLGSI--LHDPN-IFKHPE 410
Cdd:cd20637 275 NGclceGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGY-RTALQTFELDGFQIPKGWSV---LYSIrdTHDTApVFKDVD 350
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13449277 411 EFNPDRF-----LDADGRFRkheaFLPFSLGKRVCLGEGLAKaeLFL 452
Cdd:cd20637 351 AFDPDRFgqersEDKDGRFH----YLPFGGGVRTCLGKQLAK--LFL 391
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
285-465 9.87e-15

cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes catalyze the final steps in the production of glucocorticoids and mineralocorticoids that takes place in the adrenal gland. There are two human CYP11B isoforms: Cyb11B1 (11-beta-hydroxylase or P45011beta), which catalyzes the final step of cortisol synthesis by a one-step reaction from 11-deoxycortisol; and CYP11B2 (aldosterone synthase or P450aldo), which catalyzes three steps in the synthesis of aldosterone. The CYP11B subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410737 [Multi-domain]  Cd Length: 428  Bit Score: 76.03  E-value: 9.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 TEFTNKNMLMTVIYLLFagtmtvsttvgyTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTRLPYTDAVLHEAQRLL 364
Cdd:cd20644 238 TELTAGGVDTTAFPLLF------------TLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLY 305
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 365 alvPMGI--PRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAfLPFSLGKRVCLG 442
Cdd:cd20644 306 ---PVGItvQRVPSSDLVLQNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH-LAFGFGMRQCLG 381
                       170       180
                ....*....|....*....|...
gi 13449277 443 EGLAKAELFLFFTTILQAFSLES 465
Cdd:cd20644 382 RRLAEAEMLLLLMHVLKNFLVET 404
PLN02774 PLN02774
brassinosteroid-6-oxidase
265-456 2.43e-14

brassinosteroid-6-oxidase


Pssm-ID: 178373  Cd Length: 463  Bit Score: 75.20  E-value: 2.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  265 ARDLVDAFLLKMAQEEQNPGTEF-----------------TNKNMLMTVIYLLFAGTMTVSTTVgytlLLLMKYPHVQKW 327
Cdd:PLN02774 221 ARKNIVRMLRQLIQERRASGETHtdmlgylmrkegnryklTDEEIIDQIITILYSGYETVSTTS----MMAVKYLHDHPK 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  328 VREELNRE---LGAGQAP----SLGDRTRLPYTDAVLHEAQRLLALVPmGIPRTLMRTTRFRGYTLPQGTEVFPLLGSIL 400
Cdd:PLN02774 297 ALQELRKEhlaIRERKRPedpiDWNDYKSMRFTRAVIFETSRLATIVN-GVLRKTTQDMELNGYVIPKGWRIYVYTREIN 375
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 13449277  401 HDPNIFKHPEEFNPDRFLDADgrFRKHEAFLPFSLGKRVCLGEGLAKAEL--FL-FFTT 456
Cdd:PLN02774 376 YDPFLYPDPMTFNPWRWLDKS--LESHNYFFLFGGGTRLCPGKELGIVEIstFLhYFVT 432
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
234-450 3.19e-14

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


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 74.73  E-value: 3.19e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 234 HKQLLHHVSTL-----------------AAFTVRQVQQ------HQGNLDASGPAR-----DLVDAFLLkmAQEEQnpGT 285
Cdd:cd20679 163 QQQLLLHLDFLyyltadgrrfrracrlvHDFTDAVIQErrrtlpSQGVDDFLKAKAksktlDFIDVLLL--SKDED--GK 238
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 286 EFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELnRELGAGQAP---SLGDRTRLPYTDAVLHEAQR 362
Cdd:cd20679 239 ELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEV-QELLKDREPeeiEWDDLAQLPFLTMCIKESLR 317
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 363 LLALVPMgIPRTLMRTTRFR-GYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRKHEAFLPFSLGKRVCL 441
Cdd:cd20679 318 LHPPVTA-ISRCCTQDIVLPdGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGRSPLAFIPFSAGPRNCI 396

                ....*....
gi 13449277 442 GEGLAKAEL 450
Cdd:cd20679 397 GQTFAMAEM 405
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
264-461 7.24e-14

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


Pssm-ID: 410718 [Multi-domain]  Cd Length: 369  Bit Score: 72.97  E-value: 7.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAfllkMAQEEQNpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREElnrelgagqaPS 343
Cdd:cd20625 179 PGDDLISA----LVAAEED-GDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLRAD----------PE 243
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 LgdrtrlpyTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRfldADGR 423
Cdd:cd20625 244 L--------IPAAVEELLRYDSPVQL-TARVALEDVEIGGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITR---APNR 311
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13449277 424 frkHeafLPFSLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd20625 312 ---H---LAFGAGIHFCLGAPLARLEAEIALRALLRRF 343
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
65-466 1.04e-13

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: 72.70  E-value: 1.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  65 GPVFTIYLGpWRPVVVLVGQEAVREALGGqaeefSGRGTVAM------LEGTFDGHGVFFSNGERWRQLRK-----FTML 133
Cdd:cd20615   1 GPIYRIWSG-PTPEIVLTTPEHVKEFYRD-----SNKHHKAPnnnsgwLFGQLLGQCVGLLSGTDWKRVRKvfdpaFSHS 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 134 ALRdlgmgkrEGEELIQAEARCLVE--TFQGTEGRPFDpsLLLAQATSN----VVCSLLFGLRFsyeDKEFQAVVRAAG- 206
Cdd:cd20615  75 AAV-------YYIPQFSREARKWVQnlPTNSGDGRRFV--IDPAQALKFlpfrVIAEILYGELS---PEEKEELWDLAPl 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 207 -GTLLGVSSQGGQTyeMFSWFlRPLPGPHKQLLHHVST-LAAFTVRQVQQHQGNlDASGPARDLVDAFllkmaqeeqNPG 284
Cdd:cd20615 143 rEELFKYVIKGGLY--RFKIS-RYLPTAANRRLREFQTrWRAFNLKIYNRARQR-GQSTPIVKLYEAV---------EKG 209
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 285 TeFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREEL--NRELgagQAPSLGDRTRLpyTDAVLH---- 358
Cdd:cd20615 210 D-ITFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIsaAREQ---SGYPMEDYILS--TDTLLAycvl 283
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 359 EAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLDAD-GRFRKHeaFLPFSLG 436
Cdd:cd20615 284 ESLRLRPLLAFSVPESSPTDKIIGGYRIPANTPVVVDTYALNINNPFWgPDGEAYRPERFLGISpTDLRYN--FWRFGFG 361
                       410       420       430
                ....*....|....*....|....*....|
gi 13449277 437 KRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:cd20615 362 PRKCLGQHVADVILKALLAHLLEQYELKLP 391
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
266-450 1.39e-13

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


Pssm-ID: 410702 [Multi-domain]  Cd Length: 370  Bit Score: 72.12  E-value: 1.39e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 266 RDLVDAFLLKMAQEEQ-NPGTE--------------FTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVRE 330
Cdd:cd11080 153 AEQLSQYLLPVIEERRvNPGSDlisilctaeyegeaLSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQLAAVRA 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 331 elnrelgagqapslgDRTRLPytdAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPE 410
Cdd:cd11080 233 ---------------DRSLVP---RAIAETLRYHPPVQL-IPRQASQDVVVSGMEIKKGTTVFCLIGAANRDPAAFEDPD 293
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 13449277 411 EFNPDRfldADGRFRKheAF------LPFSLGKRVCLGEGLAKAEL 450
Cdd:cd11080 294 TFNIHR---EDLGIRS--AFsgaadhLAFGSGRHFCVGAALAKREI 334
PLN02971 PLN02971
tryptophan N-hydroxylase
267-466 2.98e-13

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 71.99  E-value: 2.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  267 DLVDAFLlKMAQEEQNPgtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGD 346
Cdd:PLN02971 306 DFLDIFI-SIKDEAGQP--LLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMINKPEILHKAMEEIDRVVGKERFVQESD 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  347 RTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRK 426
Cdd:PLN02971 383 IPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLGRNPKVWSDPLSFKPERHLNECSEVTL 462
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 13449277  427 HE---AFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESP 466
Cdd:PLN02971 463 TEndlRFISFSTGKRGCAAPALGTAITTMMLARLLQGFKWKLA 505
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
250-453 3.84e-13

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


Pssm-ID: 215600  Cd Length: 452  Bit Score: 71.31  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  250 RQVQQHQGNLDASGPARDLVDAfLLKMAQEEQNpgTEFTNKNMlmtvIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVR 329
Cdd:PLN03141 217 KRRAMKNKEEDETGIPKDVVDV-LLRDGSDELT--DDLISDNM----IDMMIPGEDSVPVLMTLAVKFLSDCPVALQQLT 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  330 EElNRELGAGQAPS-----LGDRTRLPYTDAVLHEAQRLLALVpMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPN 404
Cdd:PLN03141 290 EE-NMKLKRLKADTgeplyWTDYMSLPFTQNVITETLRMGNII-NGVMRKAMKDVEIKGYLIPKGWCVLAYFRSVHLDEE 367
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 13449277  405 IFKHPEEFNPDRFLDADGrfrKHEAFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:PLN03141 368 NYDNPYQFNPWRWQEKDM---NNSSFTPFGGGQRLCPGLDLARLEASIF 413
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
313-474 1.01e-12

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


Pssm-ID: 410728  Cd Length: 410  Bit Score: 69.65  E-value: 1.01e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 313 YTLLLLMKYPHVQKWVREELNRELG-AGQAP---SLGDRTRLPYTDAVLHEAQRLLAlvPMGIPRTLMRTTRFRGYTLPQ 388
Cdd:cd20635 232 WTLAFILSHPSVYKKVMEEISSVLGkAGKDKikiSEDDLKKMPYIKRCVLEAIRLRS--PGAITRKVVKPIKIKNYTIPA 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 389 GTEVF--PLLgsiLH-DPNIFKHPEEFNPDRFLDADgrFRKH---EAFLPFSLGKRVCLGEGLAKAELFLFFTTILQA-- 460
Cdd:cd20635 310 GDMLMlsPYW---AHrNPKYFPDPELFKPERWKKAD--LEKNvflEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKyd 384
                       170
                ....*....|....*
gi 13449277 461 FSLESPCP-PDTLSL 474
Cdd:cd20635 385 FTLLDPVPkPSPLHL 399
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
299-477 1.28e-12

cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and bacterial CYPs including Saccharopolyspora erythraea P450 EryK, Saccharolobus solfataricus cytochrome P450 119 (CYP119), Picrophilus torridus CYP231A2, Bacillus subtilis CYP109, Streptomyces himastatinicus HmtT and HmtN, and Bacillus megaterium CYP106A2, among others. EryK, also called erythromycin C-12 hydroxylase, is active during the final steps of erythromycin A (ErA) biosynthesis. CYP106A2 catalyzes the hydroxylation of a variety of 3-oxo-delta(4)-steroids such as progesterone and deoxycorticosterone, mainly in the 15beta-position. It is also capable of hydroxylating a variety of terpenoids. HmtT and HmtN is involved in the post-tailoring of the cyclohexadepsipeptide backbone during the biosynthesis of the himastatin antibiotic. The EryK-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 69.17  E-value: 1.28e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 299 LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREelnrelgagqapslgDRTRLPytdAVLHEAQRLLALVpMGIPRTLMRT 378
Cdd:cd11032 206 LLIAGHETTTNLLGNAVLCLDEDPEVAARLRA---------------DPSLIP---GAIEEVLRYRPPV-QRTARVTTED 266
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 379 TRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRfldadgRFRKHeafLPFSLGKRVCLGEGLAKAELFLFFTTIL 458
Cdd:cd11032 267 VELGGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR------NPNPH---LSFGHGIHFCLGAPLARLEARIALEALL 337
                       170
                ....*....|....*....
gi 13449277 459 QAFSLESPCPPDTLSLKPT 477
Cdd:cd11032 338 DRFPRIRVDPDVPLELIDS 356
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
267-482 2.44e-12

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: 68.55  E-value: 2.44e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 267 DLVDAFLlKMAQEEQNPgtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGD 346
Cdd:cd20658 216 DWLDVFI-TLKDENGNP--LLTPDEIKAQIKELMIAAIDNPSNAVEWALAEMLNQPEILRKATEELDRVVGKERLVQESD 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 347 RTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVF---PLLGsilHDPNIFKHPEEFNPDRFLDADGR 423
Cdd:cd20658 293 IPNLNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLlsrYGLG---RNPKVWDDPLKFKPERHLNEDSE 369
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13449277 424 FRKHEA---FLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLESPCPPDTLSLKPTVSGLF 482
Cdd:cd20658 370 VTLTEPdlrFISFSTGRRGCPGVKLGTAMTVMLLARLLQGFTWTLPPNVSSVDLSESKDDLF 431
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
251-453 2.87e-12

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 68.24  E-value: 2.87e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 251 QVQQHQGNLDASGPARDLVDAfllkMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVRE 330
Cdd:cd20614 172 RLSQLVATARANGARTGLVAA----LIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCD 247
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 331 ELNRELGAGQAPSLGDrtRLPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPE 410
Cdd:cd20614 248 EAAAAGDVPRTPAELR--RFPLAEALFRETLRLHPPVPF-VFRRVLEEIELGGRRIPAGTHLGIPLLLFSRDPELYPDPD 324
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 13449277 411 EFNPDRFLDADGRFRKHEaFLPFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd20614 325 RFRPERWLGRDRAPNPVE-LLQFGGGPHFCLGYHVACVELVQF 366
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
266-461 4.30e-12

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


Pssm-ID: 410723 [Multi-domain]  Cd Length: 373  Bit Score: 67.45  E-value: 4.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 266 RDLVDAFLLKMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREElnRELGAGqapslg 345
Cdd:cd20630 178 QAPVEDDLLTTLLRAEEDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE--PELLRN------ 249
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 346 drtrlpytdaVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADgrfr 425
Cdd:cd20630 250 ----------ALEEVLRWDNFGKMGTARYATEDVELCGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRRDPNAN---- 315
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 13449277 426 kheafLPFSLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd20630 316 -----IAFGYGPHFCIGAALARLELELAVSTLLRRF 346
PLN00168 PLN00168
Cytochrome P450; Provisional
57-461 4.97e-12

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 68.05  E-value: 4.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277   57 LMRLSKKYGPVFTIYLGPwRPVVVLVGQEAVREALGGQAEEFSGRGTVA--MLEGTFDGHGVFFSNGERWRQLRKftMLA 134
Cdd:PLN00168  63 LRRLIARYGPVVSLRVGS-RLSVFVADRRLAHAALVERGAALADRPAVAssRLLGESDNTITRSSYGPVWRLLRR--NLV 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  135 LRDLGMGKREGEELIQAEARCLVETFQGTEGRPFDPSLLLAQATSNVVCSLL---FGLRFsyEDKEFQAVVRAAGGTLLG 211
Cdd:PLN00168 140 AETLHPSRVRLFAPARAWVRRVLVDKLRREAEDAAAPRVVETFQYAMFCLLVlmcFGERL--DEPAVRAIAAAQRDWLLY 217
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  212 VSSQGGQ-------TYEMFSWFLRP-LPGPHKQLLHHVSTLAAFTVRQVQQHQGNLDASGPA---RDLVDAFLLKMAQEE 280
Cdd:PLN00168 218 VSKKMSVfaffpavTKHLFRGRLQKaLALRRRQKELFVPLIDARREYKNHLGQGGEPPKKETtfeHSYVDTLLDIRLPED 297
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  281 QNpgTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQ-APSLGDRTRLPYTDAVLHE 359
Cdd:PLN00168 298 GD--RALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKLHDEIKAKTGDDQeEVSEEDVHKMPYLKAVVLE 375
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  360 AQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFL------DADGRFRKHEAFLPF 433
Cdd:PLN00168 376 GLRKHPPAHFVLPHKAAEDMEVGGYLIPKGATVNFMVAEMGRDEREWERPMEFVPERFLaggdgeGVDVTGSREIRMMPF 455
                        410       420
                 ....*....|....*....|....*...
gi 13449277  434 SLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:PLN00168 456 GVGRRICAGLGIAMLHLEYFVANMVREF 483
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
315-464 1.22e-11

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


Pssm-ID: 410726  Cd Length: 449  Bit Score: 66.62  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 315 LLLLMKYPHVQKWVREELNREL-GAGQAPSLGDR---------TRLPYTDAVLHEAQRLLAlVPMGIpRTLMRTTRF--- 381
Cdd:cd20633 248 LLYLLKHPEAMKAVREEVEQVLkETGQEVKPGGPlinltrdmlLKTPVLDSAVEETLRLTA-APVLI-RAVVQDMTLkma 325
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 382 --RGYTLPQGTEV--FPLLGSILhDPNIFKHPEEFNPDRFLDADGRFRK---------HEAFLPFSLGKRVCLGEGLAKA 448
Cdd:cd20633 326 ngREYALRKGDRLalFPYLAVQM-DPEIHPEPHTFKYDRFLNPDGGKKKdfykngkklKYYNMPWGAGVSICPGRFFAVN 404
                       170
                ....*....|....*.
gi 13449277 449 ELFLFFTTILQAFSLE 464
Cdd:cd20633 405 EMKQFVFLMLTYFDLE 420
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
264-461 2.09e-10

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


Pssm-ID: 410700 [Multi-domain]  Cd Length: 380  Bit Score: 62.24  E-value: 2.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAfLLKMAQEEqnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREelnrelgagqaps 343
Cdd:cd11078 186 PRDDLISD-LLAAADGD---GERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRA------------- 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 lgDRTRLPytDAVlHEAQRLLALVPmGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRfldadGR 423
Cdd:cd11078 249 --DPSLIP--NAV-EETLRYDSPVQ-GLRRTATRDVEIGGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR-----PN 317
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13449277 424 FRKHeafLPFSLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd11078 318 ARKH---LTFGHGIHFCLGAALARMEARIALEELLRRL 352
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
296-464 3.83e-10

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 62.02  E-value: 3.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  296 VIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGDRTR-LPYTDAVLHEAQRLLALVPMgiprt 374
Cdd:PLN02426 298 VVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNQEAASFEEMKeMHYLHAALYESMRLFPPVQF----- 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  375 lmrTTRF--RGYTLPQGTEVfpllgsiLHDPNIFKHP--------------EEFNPDRFLDaDGRFRKHEAF-LP-FSLG 436
Cdd:PLN02426 373 ---DSKFaaEDDVLPDGTFV-------AKGTRVTYHPyamgrmeriwgpdcLEFKPERWLK-NGVFVPENPFkYPvFQAG 441
                        170       180
                 ....*....|....*....|....*...
gi 13449277  437 KRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:PLN02426 442 LRVCLGKEMALMEMKSVAVAVVRRFDIE 469
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
264-478 5.08e-10

cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial cytochrome P450s from families 107 (CYP107), 154 (CYP154), 197 (CYP197), and similar proteins. Among the members of this group are: Pseudonocardia autotrophica vitamin D(3) 25-hydroxylase (also known as CYP197A; EC 1.14.15.15) that catalyzes the hydroxylation of vitamin D(3) into 25-hydroxyvitamin D(3) and 1-alpha,25-dihydroxyvitamin D(3), its physiologically active forms; Saccharopolyspora erythraea CYP107A1, also called P450eryF or 6-deoxyerythronolide B hydroxylase (EC 1.14.15.35), that catalyzes the conversion of 6-deoxyerythronolide B (6-DEB) to erythronolide B (EB) by the insertion of an oxygen at the 6S position of 6-DEB; Bacillus megaterium CYP107DY1 that displays C6-hydroxylation activity towards mevastatin to produce pravastatin; Streptomyces coelicolor CYP154C1 that shows activity towards 12- and 14-membered ring macrolactones in vitro and may be involved in catalyzing the site-specific oxidation of the precursors to macrolide antibiotics, which introduces regiochemical diversity into the macrolide ring system; and Nocardia farcinica CYP154C5 that acts on steroids with regioselectivity and stereoselectivity, converting various pregnans and androstans to yield 16 alpha-hydroxylated steroid products. Bacillus subtilis CYP107H1 is not included in this group. The CYP107-like group belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410655 [Multi-domain]  Cd Length: 384  Bit Score: 61.01  E-value: 5.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAFLLkmAQEEqnpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREElnrelgagqaPS 343
Cdd:cd11029 189 PGDDLLSALVA--ARDE---GDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRAD----------PE 253
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 LgdrtrlpyTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRfldADGR 423
Cdd:cd11029 254 L--------WPAAVEELLRYDGPVALATLRFATEDVEVGGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR---DANG 322
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13449277 424 frkHeafLPFSLGKRVCLGEGLAKAELFLFFTTILQAF-SLESPCPPDTLSLKPTV 478
Cdd:cd11029 323 ---H---LAFGHGIHYCLGAPLARLEAEIALGALLTRFpDLRLAVPPDELRWRPSF 372
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
313-488 5.18e-10

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


Pssm-ID: 410724 [Multi-domain]  Cd Length: 451  Bit Score: 61.24  E-value: 5.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 313 YTLLLLMKYPHVQKWVREELNRELG-AGQAPSLG----DRTR-----LPYTDAVLHEAQRLLAlVPMGIpRTLMRTTRF- 381
Cdd:cd20631 249 WSLFYLLRCPEAMKAATKEVKRTLEkTGQKVSDGgnpiVLTReqlddMPVLGSIIKEALRLSS-ASLNI-RVAKEDFTLh 326
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 382 ----RGYTLPQGtEVFPLLGSILH-DPNIFKHPEEFNPDRFLDA----------DGRFRKHeAFLPFSLGKRVCLGEGLA 446
Cdd:cd20631 327 ldsgESYAIRKD-DIIALYPQLLHlDPEIYEDPLTFKYDRYLDEngkekttfykNGRKLKY-YYMPFGSGTSKCPGRFFA 404
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13449277 447 KAELFLFFTTILQAFSLE-----SPCPPdtlsLKPTVSGLFNIPPAF 488
Cdd:cd20631 405 INEIKQFLSLMLCYFDMElldgnAKCPP----LDQSRAGLGILPPTH 447
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
281-477 7.19e-10

cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or estrogen synthetase (EC 1.14.14.14), catalyzes the formation of aromatic C18 estrogens from C19 androgens. The CYP19A1 subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410709 [Multi-domain]  Cd Length: 414  Bit Score: 60.84  E-value: 7.19e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 281 QNPGtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGaGQAPSLGDRTRLPYTDAVLHEA 360
Cdd:cd20616 215 QKRG-ELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLG-ERDIQNDDLQKLKVLENFINES 292
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 361 QRLLALVPMgIPRTLMRTTRFRGYTLPQGTEVFPLLGSiLHDPNIFKHPEEFNPDRFL-DADGRFrkheaFLPFSLGKRV 439
Cdd:cd20616 293 MRYQPVVDF-VMRKALEDDVIDGYPVKKGTNIILNIGR-MHRLEFFPKPNEFTLENFEkNVPSRY-----FQPFGFGPRS 365
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 13449277 440 CLGEGLAKAELFLFFTTILQAFSLespCPPDT-----------LSLKPT 477
Cdd:cd20616 366 CVGKYIAMVMMKAILVTLLRRFQV---CTLQGrcveniqktndLSLHPD 411
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
291-448 7.48e-10

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 60.43  E-value: 7.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 291 NMLMTVIyllfAGTMTVSTTVGYTLLLLMKYPHVQKWvrEELNRelgAGQAPSLGDRTRLPYtdaVLhEAQRLLALVPmG 370
Cdd:cd20612 191 NVLGTAV----GGVPTQSQAFAQILDFYLRRPGAAHL--AEIQA---LARENDEADATLRGY---VL-EALRLNPIAP-G 256
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 371 IPRTLMRTTRF-----RGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDrfldadgrfRKHEAFLPFSLGKRVCLGEGL 445
Cdd:cd20612 257 LYRRATTDTTVadgggRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLD---------RPLESYIHFGHGPHQCLGEEI 327

                ...
gi 13449277 446 AKA 448
Cdd:cd20612 328 ARA 330
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
62-480 1.12e-09

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


Pssm-ID: 410694 [Multi-domain]  Cd Length: 424  Bit Score: 60.35  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  62 KKYGP-VFTIYLGPWRP------VVVLVGQEAV-----------REALGG----QAEEFSGRGTVAMLegtfdghgvfFS 119
Cdd:cd11071   5 EKYKStVFRVNMPPGPPissdprVVALLDAKSFpvlfdnskvekEDVFGGtympSTSFTGGYRVLPYL----------DT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 120 NGERWRQLRKFTMLALrdlgmgKREGEELIQAEARCLVETFQ-----GTEGRPFDPSLLLAQATSNVVCSLLFGLRFSYE 194
Cdd:cd11071  75 SEPKHAKLKAFLFELL------KSRSSRFIPEFRSALSELFDkweaeLAKKGKASFNDDLEKLAFDFLFRLLFGADPSET 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 195 DKEFQAVVRA---AGGTLLGVSSQGgqtyemfswflrpLPGPHKQLLHHVSTLAAFTVrqvqqhqgnldaSGPARDLVDA 271
Cdd:cd11071 149 KLGSDGPDALdkwLALQLAPTLSLG-------------LPKILEELLLHTFPLPFFLV------------KPDYQKLYKF 203
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 272 F------LLKMAQEEQNPGTEFTNkNMLMTVIYLLFAGTMTVSTTVGYTLLLLMkyPHVQKWVREELNRELGAGQAPSLG 345
Cdd:cd11071 204 FanagleVLDEAEKLGLSREEAVH-NLLFMLGFNAFGGFSALLPSLLARLGLAG--EELHARLAEEIRSALGSEGGLTLA 280
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 346 DRTRLPYTDAVLHEAQRLLALVPM--GIPRtlmrttrfRGYTLPQGTEVFP------LLGSI---LHDPNIFKHPEEFNP 414
Cdd:cd11071 281 ALEKMPLLKSVVYETLRLHPPVPLqyGRAR--------KDFVIESHDASYKikkgelLVGYQplaTRDPKVFDNPDEFVP 352
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 415 DRFLDADGRFRKH-------EAFLPfSLGKRVC----LGEGLAK---AELFLFFttilQAFSLEspcpPDTLSLKPTVSG 480
Cdd:cd11071 353 DRFMGEEGKLLKHliwsngpETEEP-TPDNKQCpgkdLVVLLARlfvAELFLRY----DTFTIE----PGWTGKKLSVTV 423
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
314-464 1.46e-09

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


Pssm-ID: 410717 [Multi-domain]  Cd Length: 376  Bit Score: 59.78  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 314 TLLLLMKYPHVQKWVREElnrelgAGQAPSLGDRtrlPYTDAVLHEAQRLLALVPMgIPRTLMRTTRFRGYTLPQGTEvF 393
Cdd:cd20624 214 ALALLAAHPEQAARAREE------AAVPPGPLAR---PYLRACVLDAVRLWPTTPA-VLRESTEDTVWGGRTVPAGTG-F 282
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13449277 394 PLLGSILH-DPNIFKHPEEFNPDRFLDadGRFRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLE 464
Cdd:cd20624 283 LIFAPFFHrDDEALPFADRFVPEIWLD--GRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEID 352
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
110-455 1.77e-09

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 59.79  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  110 TFDGHGVFFSNGERWRQLRK-----FTMLALRDLGMGK-RE-----GEELIQAearclvetfqGTEGRPFDPSLLLAQAT 178
Cdd:PLN03195 109 VLLGDGIFNVDGELWRKQRKtasfeFASKNLRDFSTVVfREyslklSSILSQA----------SFANQVVDMQDLFMRMT 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  179 SNVVCSLLFG-----LRFSYEDKEFQAVVRAAGGTLlgvssqggqTYEMFS--WFLRPL--PGPHKQLLHHVSTLAAFTV 249
Cdd:PLN03195 179 LDSICKVGFGveigtLSPSLPENPFAQAFDTANIIV---------TLRFIDplWKLKKFlnIGSEALLSKSIKVVDDFTY 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  250 RQVQQHQGNLDASGPARDLVDAFLL-KMAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWV 328
Cdd:PLN03195 250 SVIRRRKAEMDEARKSGKKVKHDILsRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKL 329
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  329 REEL-------NRELGAGQAPSLGDR-------------TRLPYTDAVLHEAQRLLALVPMGiPRTLMRTTrfrgyTLPQ 388
Cdd:PLN03195 330 YSELkalekerAKEEDPEDSQSFNQRvtqfaglltydslGKLQYLHAVITETLRLYPAVPQD-PKGILEDD-----VLPD 403
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  389 GTEVfPLLGSILHDP--------NIFKHPEEFNPDRFLDaDGRFRKHEA--FLPFSLGKRVCLGEG-------LAKAELF 451
Cdd:PLN03195 404 GTKV-KAGGMVTYVPysmgrmeyNWGPDAASFKPERWIK-DGVFQNASPfkFTAFQAGPRICLGKDsaylqmkMALALLC 481

                 ....
gi 13449277  452 LFFT 455
Cdd:PLN03195 482 RFFK 485
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
315-464 3.34e-09

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 59.00  E-value: 3.34e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 315 LLLLMKYPHVQKWVREELNREL---GAGQAPSLGDRTRL----PYTDAVLHEAQRLLAlVPMgIPRTL-----MRTTRFR 382
Cdd:cd20634 245 LLFLLKHPEAMAAVRGEIQRIKhqrGQPVSQTLTINQELldntPVFDSVLSETLRLTA-APF-ITREVlqdmkLRLADGQ 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 383 GYTLPQGTEV--FPLLgSILHDPNIFKHPEEFNPDRFLDADG----RFRKHEAFL-----PFSLGKRVCLGEGLAKAELF 451
Cdd:cd20634 323 EYNLRRGDRLclFPFL-SPQMDPEIHQEPEVFKYDRFLNADGtekkDFYKNGKRLkyynmPWGAGDNVCIGRHFAVNSIK 401
                       170
                ....*....|...
gi 13449277 452 LFFTTILQAFSLE 464
Cdd:cd20634 402 QFVFLILTHFDVE 414
PLN03018 PLN03018
homomethionine N-hydroxylase
267-494 4.29e-09

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 58.87  E-value: 4.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  267 DLVDAFLlkmAQEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQAPSLGD 346
Cdd:PLN03018 293 DWLDTFI---TLKDQNGKYLVTPDEIKAQCVEFCIAAIDNPANNMEWTLGEMLKNPEILRKALKELDEVVGKDRLVQESD 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  347 RTRLPYTDAVLHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLDADGRFRK 426
Cdd:PLN03018 370 IPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVCRPGLGRNPKIWKDPLVYEPERHLQGDGITKE 449
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13449277  427 ------HEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFS--LESPCPPdtLSLKPTVSGLFNIPPaFQLQVRP 494
Cdd:PLN03018 450 vtlvetEMRFVSFSTGRRGCVGVKVGTIMMVMMLARFLQGFNwkLHQDFGP--LSLEEDDASLLMAKP-LLLSVEP 522
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
352-446 6.45e-09

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


Pssm-ID: 410690 [Multi-domain]  Cd Length: 400  Bit Score: 57.92  E-value: 6.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 352 YTDAVLHEAQRLLALVPM--GIPRtlmRTTRFRGYTLPQGTEVfpLLG--SILHDPNIFKHPEEFNPDRFLDADG-RFRk 426
Cdd:cd11067 264 YAEAFVQEVRRFYPFFPFvgARAR---RDFEWQGYRFPKGQRV--LLDlyGTNHDPRLWEDPDRFRPERFLGWEGdPFD- 337
                        90       100
                ....*....|....*....|....*
gi 13449277 427 heaFLP-----FSLGKRvCLGEGLA 446
Cdd:cd11067 338 ---FIPqgggdHATGHR-CPGEWIT 358
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
264-462 7.36e-09

cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces sp. P450sky (also called CYP163B3), Sphingopyxis macrogoltabida P450pyr hydroxylase, Novosphingobium aromaticivorans CYP108D1, Pseudomonas sp. cytochrome P450-Terp (P450terp), and Amycolatopsis balhimycina P450 OxyD, as well as several Mycobacterium proteins CYP124, CYP125, CYP126, and CYP142. P450sky is involved in the hydroxylation of three beta-hydroxylated amino acid precursors required for the biosynthesis of the cyclic depsipeptide skyllamycin. P450pyr hydroxylase is an active and selective catalyst for the regio- and stereo-selective hydroxylation at non-activated carbon atoms with a broad substrate range. P450terp catalyzes the hydroxylation of alpha-terpineol as part of its catabolic assimilation. OxyD is involved in beta-hydroxytyrosine formation during vancomycin biosynthesis. CYP124 is a methyl-branched lipid omega-hydroxylase while CYP142 is a cholesterol 27-oxidase with likely roles in host response modulation and cholesterol metabolism. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 57.54  E-value: 7.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAfllkMAQEEQNpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREelnrelgagqaps 343
Cdd:cd11033 187 PGDDLISV----LANAEVD-GEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHPDQWERLRA------------- 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 lgDRTRLP--------YTDAVLHeaqrllalvpMGipRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPD 415
Cdd:cd11033 249 --DPSLLPtaveeilrWASPVIH----------FR--RTATRDTELGGQRIRAGDKVVLWYASANRDEEVFDDPDRFDIT 314
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 13449277 416 RfldadgRFRKHeafLPFSLGKRVCLGEGLAKAELFLFFTTILQAFS 462
Cdd:cd11033 315 R------SPNPH---LAFGGGPHFCLGAHLARLELRVLFEELLDRVP 352
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
264-477 9.76e-09

cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Streptomyces coelicolor CYP158A1 and CYP158A2, Streptomyces natalensis PimD (also known as CYP107E), Mycobacterium tuberculosis CYP121, and Micromonospora griseorubida MycG (also known as CYP107B). CYP158A1 and CYP158A2 catalyze an unusual oxidative C-C coupling reaction to polymerize flaviolin and form highly conjugated pigments; CYP158A2 produces three isomers of biflaviolin and one triflaviolin while CYP158A1 produces only two isomers of biflaviolin. PimD is a cytochrome P450 monooxygenase with native epoxidase activity that is critical in the biosynthesis of the polyene macrolide antibiotic pimaricin. CYP121 is essential for the viability of M. tuberculosis and is a novel drug target for the inhibition of mycobacterial growth. MycG catalyzes both hydroxylation and epoxidation reactions in the biosynthesis of the 16-membered ring macrolide antibiotic mycinamicin II. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 57.19  E-value: 9.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAFLlkmaqEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREElnrelgagqaPS 343
Cdd:cd11031 184 PGDDLLSALV-----AARDDDDRLSEEELVTLAVGLLVAGHETTASQIGNGVLLLLRHPEQLARLRAD----------PE 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 LgdrtrLPytDAVlheaQRLLALVP----MGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDrfld 419
Cdd:cd11031 249 L-----VP--AAV----EELLRYIPlgagGGFPRYATEDVELGGVTIRAGEAVLVSLNAANRDPEVFPDPDRLDLD---- 313
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 13449277 420 adgrfRKHEAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAF-SLESPCPPDTLSLKPT 477
Cdd:cd11031 314 -----REPNPHLAFGHGPHHCLGAPLARLELQVALGALLRRLpGLRLAVPEEELRWREG 367
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
264-461 2.04e-08

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 56.19  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAFLlkmaqEEQNPGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPhvqkwvreELNRELGAGqaPS 343
Cdd:cd11034 168 PRDDLISRLI-----EGEIDGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHP--------EDRRRLIAD--PS 232
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 LGDRtrlpytdAVlHEAQRLLALVpMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFLdadgr 423
Cdd:cd11034 233 LIPN-------AV-EEFLRFYSPV-AGLARTVTQEVEVGGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTP----- 298
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 13449277 424 fRKHeafLPFSLGKRVCLGEGLAKAELFLFFTTILQAF 461
Cdd:cd11034 299 -NRH---LAFGSGVHRCLGSHLARVEARVALTEVLKRI 332
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
265-450 6.63e-08

cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus P450 monooxygenase AurH which is uniquely capable of forming a homochiral tetrahydrofuran ring, a vital component of the polyketide antibiotic aureothin. AurH catalyzes an unprecedented tandem oxygenation process: first, it catalyzes an asymmetric hydroxylation of deoxyaureothin to yield (7R)-7-hydroxydeoxyaureothin as an intermediate; and second, it mediates another C-O bond formation that leads to O-heterocyclization. The AurH-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 54.68  E-value: 6.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 265 ARDLVDAFLLKMAQEEQNpGTEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPhvQKWvreelnRELGAGqaPSL 344
Cdd:cd11038 189 RAEPGDDLISTLVAAEQD-GDRLSDEELRNLIVALLFAGVDTTRNQLGLAMLTFAEHP--DQW------RALRED--PEL 257
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 345 GDRtrlpytdAVlHEAQRLLALVPMGIpRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIfkhpeeFNPDRFlDADgrf 424
Cdd:cd11038 258 APA-------AV-EEVLRWCPTTTWAT-REAVEDVEYNGVTIPAGTVVHLCSHAANRDPRV------FDADRF-DIT--- 318
                       170       180
                ....*....|....*....|....*.
gi 13449277 425 RKHEAFLPFSLGKRVCLGEGLAKAEL 450
Cdd:cd11038 319 AKRAPHLGFGGGVHHCLGAFLARAEL 344
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
264-477 1.58e-07

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


Pssm-ID: 410656 [Multi-domain]  Cd Length: 381  Bit Score: 53.30  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 264 PARDLVDAfllkMAQEEQNPGtEFTNKNMLMTVIYLLFAGTMTVSTTVGYTLLLLMKYPhvqkwvreelnrelgaGQAPS 343
Cdd:cd11030 186 PGDDLLSR----LVAEHGAPG-ELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHP----------------EQLAA 244
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 344 L-GDRTRLPytDAVlHEAQRLLALVPMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRfldadg 422
Cdd:cd11030 245 LrADPSLVP--GAV-EELLRYLSIVQDGLPRVATEDVEIGGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR------ 315
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 13449277 423 RFRKHeafLPFSLGKRVCLGEGLAKAELFLFFTTILQAF-SLESPCPPDTLSLKPT 477
Cdd:cd11030 316 PARRH---LAFGHGVHQCLGQNLARLELEIALPTLFRRFpGLRLAVPAEELPFRPD 368
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
299-461 1.25e-06

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


Pssm-ID: 410663 [Multi-domain]  Cd Length: 371  Bit Score: 50.66  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 299 LLFAGTMTVSTTVGYTLLLLMKYPhvQKW--VREElnrelgagqaPSLgdrtrLPytdAVLHEAQRLLALVPmGIPRTLM 376
Cdd:cd11037 210 YLSAGLDTTISAIGNALWLLARHP--DQWerLRAD----------PSL-----AP---NAFEEAVRLESPVQ-TFSRTTT 268
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 377 RTTRFRGYTLPQGTEVFPLLGSILHDPNIFKhpeefNPDRFlDADGRFRKHeafLPFSLGKRVCLGEGLAKAELflffTT 456
Cdd:cd11037 269 RDTELAGVTIPAGSRVLVFLGSANRDPRKWD-----DPDRF-DITRNPSGH---VGFGHGVHACVGQHLARLEG----EA 335

                ....*
gi 13449277 457 ILQAF 461
Cdd:cd11037 336 LLTAL 340
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
295-440 1.31e-06

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


Pssm-ID: 410720 [Multi-domain]  Cd Length: 394  Bit Score: 50.59  E-value: 1.31e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 295 TVIYLLfAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAGQApSLGDRTRLPYTDAVLHEAQRLLALVPMGiPRT 374
Cdd:cd20627 207 SMIFSL-AGCVITANLCTWAIYFLTTSEEVQKKLYKEVDQVLGKGPI-TLEKIEQLRYCQQVLCETVRTAKLTPVS-ARL 283
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13449277 375 LMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRFldADGRFRKHEAFLPFSlGKRVC 440
Cdd:cd20627 284 QELEGKVDQHIIPKETLVLYALGVVLQDNTTWPLPYRFDPDRF--DDESVMKSFSLLGFS-GSQEC 346
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
265-453 2.02e-06

P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with similarity to Pseudomonas putida P450cam and Cyp101 proteins from Novosphingobium aromaticivorans such as CYP101C1 and CYP101D2. P450cam catalyzes the hydroxylation of camphor in a process that involves two electron transfers from the iron-sulfur protein, putidaredoxin. CYP101D2 is capable of oxidizing camphor while CYP101C1 does not bind camphor but is capable of binding and hydroxylating ionone derivatives such as alpha- and beta-ionone and beta-damascone. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 49.90  E-value: 2.02e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 265 ARDLVDAFLLKMAQEEQNPGTEFTNKNM-------------LMTVIYLLF-AGTMTVSTTVGYTLLLLMKYPHVQKWVRE 330
Cdd:cd11035 150 AQAVLDYLTPLIAERRANPGDDLISAILnaeidgrpltddeLLGLCFLLFlAGLDTVASALGFIFRHLARHPEDRRRLRE 229
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 331 ElnrelgagqaPSLgdrtrlpyTDAVLHEAQRLLALVPMgiPRTLMRTTRFRGYTLPQGTEVfpLLGSILH--DPNIFKH 408
Cdd:cd11035 230 D----------PEL--------IPAAVEELLRRYPLVNV--ARIVTRDVEFHGVQLKAGDMV--LLPLALAnrDPREFPD 287
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 13449277 409 PEEFNPDRfldadgRFRKHEAflpFSLGKRVCLGEGLAKAELFLF 453
Cdd:cd11035 288 PDTVDFDR------KPNRHLA---FGAGPHRCLGSHLARLELRIA 323
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
318-464 1.28e-05

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 47.68  E-value: 1.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 318 LMKYPHVQKWVREELNRELGA-GQAPSLGDRTRLP--------YTDAVLHEAQRLLAlVPMGIprtlmrttRF--RGYTL 386
Cdd:cd20632 242 LLRHPEALAAVRDEIDHVLQStGQELGPDFDIHLTreqldslvYLESAINESLRLSS-ASMNI--------RVvqEDFTL 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 387 PQGTE------------VFPLlgsILH-DPNIFKHPEEFNPDRFLDaDG--------RFRKHEAFL-PFSLGKRVCLGEG 444
Cdd:cd20632 313 KLESDgsvnlrkgdivaLYPQ---SLHmDPEIYEDPEVFKFDRFVE-DGkkkttfykRGQKLKYYLmPFGSGSSKCPGRF 388
                       170       180
                ....*....|....*....|
gi 13449277 445 LAKAELFLFFTTILQAFSLE 464
Cdd:cd20632 389 FAVNEIKQFLSLLLLYFDLE 408
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
289-464 7.23e-05

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 45.38  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  289 NKNMLMTVIY-LLFAGTMTVSTTVGYTLLLLMKYPHVQKWVREELNRELGAgqapslGDRTRLPYTDAVLHEAQRLLALV 367
Cdd:PLN02169 298 KDKFIRDVIFsLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN------EDLEKLVYLHAALSESMRLYPPL 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277  368 PMGIPRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIF-KHPEEFNPDRFLDADGRFRkHE---AFLPFSLGKRVCLGE 443
Cdd:PLN02169 372 PFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWgEDALDFKPERWISDNGGLR-HEpsyKFMAFNSGPRTCLGK 450
                        170       180
                 ....*....|....*....|.
gi 13449277  444 GLAKAELFLFFTTILQAFSLE 464
Cdd:PLN02169 451 HLALLQMKIVALEIIKNYDFK 471
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
299-448 1.20e-04

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


Pssm-ID: 410662 [Multi-domain]  Cd Length: 340  Bit Score: 44.02  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 299 LLFAGTMTVSTTVGYTLLLLMKYPhvqkwvrEELNRelgagqapslgDRTRLPYTDAVLHEAQRLLALVPMgIPRTLMRT 378
Cdd:cd11036 185 LAVQGAEAAAGLVGNAVLALLRRP-------AQWAR-----------LRPDPELAAAAVAETLRYDPPVRL-ERRFAAED 245
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 379 TRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNPDRfldADGRFRkheaflPFSLGKRVCLGEGLAKA 448
Cdd:cd11036 246 LELAGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR---PTARSA------HFGLGRHACLGAALARA 306
PLN02648 PLN02648
allene oxide synthase
401-423 3.20e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 43.00  E-value: 3.20e-04
                         10        20
                 ....*....|....*....|...
gi 13449277  401 HDPNIFKHPEEFNPDRFLDADGR 423
Cdd:PLN02648 387 RDPKVFDRPEEFVPDRFMGEEGE 409
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
359-448 1.36e-03

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 40.95  E-value: 1.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 359 EAQRLLAlvPMGI-PRTLMRTTRFRGYTLPQGTEVFPLLGSILHDPNIFKHPEEFNpdrfldadgRFRKHEAFLPFSLGK 437
Cdd:cd11039 252 EGLRWIS--PIGMsPRRVAEDFEIRGVTLPAGDRVFLMFGSANRDEARFENPDRFD---------VFRPKSPHVSFGAGP 320
                        90
                ....*....|.
gi 13449277 438 RVCLGEGLAKA 448
Cdd:cd11039 321 HFCAGAWASRQ 331
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
306-472 2.07e-03

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 40.42  E-value: 2.07e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 306 TVSTTVGYTLLLLMKYPHVQKWVREelnrelgagqAPSLgdrtrLPytdAVLHEAQRLLALVPmGIPRTLMRTTRFRGYT 385
Cdd:cd11079 198 TIAACVGVLVHYLARHPELQARLRA----------NPAL-----LP---AAIDEILRLDDPFV-ANRRITTRDVELGGRT 258
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13449277 386 LPQGTEVFPLLGSILHDPNIFKHPEEFNPDRflDADgrfrkheAFLPFSLGKRVCLGEGLAKAELFLFFTTILQAFSLES 465
Cdd:cd11079 259 IPAGSRVTLNWASANRDERVFGDPDEFDPDR--HAA-------DNLVYGRGIHVCPGAPLARLELRILLEELLAQTEAIT 329

                ....*..
gi 13449277 466 PCPPDTL 472
Cdd:cd11079 330 LAAGGPP 336
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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