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Conserved domains on  [gi|194390028|dbj|BAG60530|]
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unnamed protein product [Homo sapiens]

Protein Classification

cytochrome P450 family protein( domain architecture ID 1750044)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cytochrome_P450 super family cl41757
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 1-351 0e+00

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


The actual alignment was detected with superfamily member cd20678:

Pssm-ID: 477761 [Multi-domain]  Cd Length: 436  Bit Score: 762.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLE 80
Cdd:cd20678   34 AKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYDILKPYVKLMADSVRVMLDKWEKLATQDSSLE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  81 VFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTD 160
Cdd:cd20678  114 IFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTD 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 240
Cdd:cd20678  194 KVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQ 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 241 ERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKV 320
Cdd:cd20678  274 QRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAV 353

                        330       340       350
                 ....*....|....*....|....*....|...
gi 194390028 321 WPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSR 351
Cdd:cd20678  354 WPNPEVFDPLRFSPENSskRHSHAFLPFSAGPR 386
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 1-351 0e+00

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: 762.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLE 80
Cdd:cd20678   34 AKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYDILKPYVKLMADSVRVMLDKWEKLATQDSSLE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  81 VFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTD 160
Cdd:cd20678  114 IFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTD 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 240
Cdd:cd20678  194 KVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQ 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 241 ERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKV 320
Cdd:cd20678  274 QRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAV 353

                        330       340       350
                 ....*....|....*....|....*....|...
gi 194390028 321 WPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSR 351
Cdd:cd20678  354 WPNPEVFDPLRFSPENSskRHSHAFLPFSAGPR 386
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 1-351 7.64e-125

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 366.60  E-value: 7.64e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028    1 MKVILGRSD------PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLG 74
Cdd:pfam00067  55 VKEVLIKKGeefsgrPDEPWFATSRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   75 QDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLV-FSRVRNAFHQNDTIYSLTSAGRWTHRACQ 153
Cdd:pfam00067 135 EPGVIDITDLLFRAALNVICSILFGERFGSLEDPKFLELVKAVQELSSLLsSPSPQLLDLFPILKYFPGPHGRKLKRARK 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  154 LAHQHTDQVIQLRKAQLQKEGelekikrKGHLDFLDILLLAKM-ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYA 232
Cdd:pfam00067 215 KIKDLLDKLIEERRETLDSAK-------KSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYE 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  233 LATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPdGRSLPKGIMVLLSI 311
Cdd:pfam00067 288 LAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNL 366

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 194390028  312 YGLHHNPKVWPNPEVFDPFRFAP--GSAQHSHAFLPFSGGSR 351
Cdd:pfam00067 367 YALHRDPEVFPNPEEFDPERFLDenGKFRKSFAFLPFGAGPR 408
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 11-351 5.28e-52

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


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 177.01  E-value: 5.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  11 KSHGSYRFLAP--WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllgqDSPLEVFQHVSLM 88
Cdd:COG2124   65 SDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLAA----RGPVDLVEEFARP 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  89 TLDTIMKCAFSHQGSiqvDRNSqsyiqaisdlnnlvFSRVRNAFHQNDTIYSLTSAGRwTHRACQLAHQHTDQVIQLRKA 168
Cdd:COG2124  141 LPVIVICELLGVPEE---DRDR--------------LRRWSDALLDALGPLPPERRRR-ARRARAELDAYLRELIAERRA 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 169 QLQKegelekikrkghlDFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIh 248
Cdd:COG2124  203 EPGD-------------DLLSALLAAR-DDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP- 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 249 sllgdgasitwnhldqmPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFD 328
Cdd:COG2124  268 -----------------ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFD 329

                        330       340
                 ....*....|....*....|...
gi 194390028 329 PFRfapgsaqHSHAFLPFSGGSR 351
Cdd:COG2124  330 PDR-------PPNAHLPFGGGPH 345
PLN02290 PLN02290
cytokinin trans-hydroxylase
 6-351 1.49e-34

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 132.63  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   6 GRSDPKSHGSYRFlapwIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQ-DSPLEVFQH 84
Cdd:PLN02290 127 GKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESgQTEVEIGEY 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  85 VSLMTLDTIMKCAFSHQgsiqVDRNSQSYiQAISDLNNLVFSRVRNAF---------HQNDTIYSLTSagrwthracqla 155
Cdd:PLN02290 203 MTRLTADIISRTEFDSS----YEKGKQIF-HLLTVLQRLCAQATRHLCfpgsrffpsKYNREIKSLKG------------ 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 156 hqhtdQVIQLRKAQLQKEGELEKIKR-KGHLDFLDILLLAKME----NGSILSDKDLRAEVDTFMFEGHDTTASGISWIL 230
Cdd:PLN02290 266 -----EVERLLMEIIQSRRDCVEIGRsSSYGDDLLGMLLNEMEkkrsNGFNLNLQLIMDECKTFFFAGHETTALLLTWTL 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 231 YALATHPKHQERCREEIHSLLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLS 310
Cdd:PLN02290 341 MLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIP 418

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 194390028 311 IYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGSR 351
Cdd:PLN02290 419 VLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFIPFAAGPR 460
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
 1-351 0e+00

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: 762.20  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLE 80
Cdd:cd20678   34 AKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYDILKPYVKLMADSVRVMLDKWEKLATQDSSLE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  81 VFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTD 160
Cdd:cd20678  114 IFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLRNFFYHNDFIYKLSPHGRRFRRACQLAHQHTD 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 240
Cdd:cd20678  194 KVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRAEVDTFMFEGHDTTASGISWILYCLALHPEHQ 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 241 ERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKV 320
Cdd:cd20678  274 QRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISRELSKPVTFPDGRSLPAGITVSLSIYGLHHNPAV 353

                        330       340       350
                 ....*....|....*....|....*....|...
gi 194390028 321 WPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSR 351
Cdd:cd20678  354 WPNPEVFDPLRFSPENSskRHSHAFLPFSAGPR 386
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
 1-351 0e+00

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: 534.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLE 80
Cdd:cd20659   23 IKAVLKTSEPKDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVYNECTDILLEKWSKLAETGESVE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  81 VFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTD 160
Cdd:cd20659  103 VFEDISLLTLDIILRCAFSYKSNCQQTGKNHPYVAAVHELSRLVMERFLNPLLHFDWIYYLTPEGRRFKKACDYVHKFAE 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKRKgHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 240
Cdd:cd20659  183 EIIKKRRKELEDNKDEALSKRK-YLDFLDILLTARDEDGKGLTDEEIRDEVDTFLFAGHDTTASGISWTLYSLAKHPEHQ 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 241 ERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKV 320
Cdd:cd20659  262 QKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITI-DGVTLPAGTLIAINIYALHHNPTV 340

                        330       340       350
                 ....*....|....*....|....*....|...
gi 194390028 321 WPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd20659  341 WEDPEEFDPERFLPENIKkrDPFAFIPFSAGPR 373
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
 10-351 1.08e-159

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: 454.54  E-value: 1.08e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  10 PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSP-LEVFQHVSLM 88
Cdd:cd20679   46 PKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTPAFHFNILKPYVKIFNQSTNIMHAKWRRLASEGSArLDMFEHISLM 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  89 TLDTIMKCAFSHQGSIQvDRNSQsYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKA 168
Cdd:cd20679  126 TLDSLQKCVFSFDSNCQ-EKPSE-YIAAILELSALVVKRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRR 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 169 QLQKEGELE--KIKRKGH-LDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCRE 245
Cdd:cd20679  204 TLPSQGVDDflKAKAKSKtLDFIDVLLLSKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQ 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 246 EIHSLLGDGAS--ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPN 323
Cdd:cd20679  284 EVQELLKDREPeeIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPD 363

                        330       340       350
                 ....*....|....*....|....*....|
gi 194390028 324 PEVFDPFRFAPGSAQH--SHAFLPFSGGSR 351
Cdd:cd20679  364 PEVYDPFRFDPENSQGrsPLAFIPFSAGPR 393
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
 1-351 7.84e-139

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: 400.75  E-value: 7.84e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSD--PKSHGsYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSp 78
Cdd:cd20628   22 IEVILSSSKliTKSFL-YDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNENSKILVEKLKKKAGGGE- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  79 LEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSqSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQH 158
Cdd:cd20628  100 FDIFPYISLCTLDIICETAMGVKLNAQSNEDS-EYVKAVKRILEIILKRIFSPWLRFDFIFRLTSLGKEQRKALKVLHDF 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 159 TDQVIQLRKAQLQKEGELEK----IKRKGHLDFLDILLLAKMENGSiLSDKDLRAEVDTFMFEGHDTTASGISWILYALA 234
Cdd:cd20628  179 TNKVIKERREELKAEKRNSEeddeFGKKKRKAFLDLLLEAHEDGGP-LTDEDIREEVDTFMFAGHDTTASAISFTLYLLG 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 235 THPKHQERCREEIHSLLG-DGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYG 313
Cdd:cd20628  258 LHPEVQEKVYEELDEIFGdDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKL-DGYTIPKGTTVVISIYA 336

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 194390028 314 LHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd20628  337 LHRNPEYFPDPEKFDPDRFLPENSAkrHPYAYIPFSAGPR 376
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
 1-351 7.64e-125

Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative degradation of various compounds. They are particularly well known for their role in the degradation of environmental toxins and mutagens. They can be divided into 4 classes, according to the method by which electrons from NAD(P)H are delivered to the catalytic site. Sequence conservation is relatively low within the family - there are only 3 absolutely conserved residues - but their general topography and structural fold are highly conserved. The conserved core is composed of a coil termed the 'meander', a four-helix bundle, helices J and K, and two sets of beta-sheets. These constitute the haem-binding loop (with an absolutely conserved cysteine that serves as the 5th ligand for the haem iron), the proton-transfer groove and the absolutely conserved EXXR motif in helix K. While prokaryotic P450s are soluble proteins, most eukaryotic P450s are associated with microsomal membranes. their general enzymatic function is to catalyze regiospecific and stereospecific oxidation of non-activated hydrocarbons at physiological temperatures.


Pssm-ID: 395020 [Multi-domain]  Cd Length: 461  Bit Score: 366.60  E-value: 7.64e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028    1 MKVILGRSD------PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLG 74
Cdd:pfam00067  55 VKEVLIKKGeefsgrPDEPWFATSRGPFLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   75 QDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLV-FSRVRNAFHQNDTIYSLTSAGRWTHRACQ 153
Cdd:pfam00067 135 EPGVIDITDLLFRAALNVICSILFGERFGSLEDPKFLELVKAVQELSSLLsSPSPQLLDLFPILKYFPGPHGRKLKRARK 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  154 LAHQHTDQVIQLRKAQLQKEGelekikrKGHLDFLDILLLAKM-ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYA 232
Cdd:pfam00067 215 KIKDLLDKLIEERRETLDSAK-------KSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYE 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  233 LATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPdGRSLPKGIMVLLSI 311
Cdd:pfam00067 288 LAKHPEVQEKLREEIDEVIGDKRSPTYDDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNL 366

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 194390028  312 YGLHHNPKVWPNPEVFDPFRFAP--GSAQHSHAFLPFSGGSR 351
Cdd:pfam00067 367 YALHRDPEVFPNPEEFDPERFLDenGKFRKSFAFLPFGAGPR 408
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
 16-351 6.64e-118

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: 347.71  E-value: 6.64e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  16 YRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGqDSPLEVFQHVSLMTLDTIMK 95
Cdd:cd20660   38 YDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQSEILVKKLKKEVG-KEEFDIFPYITLCALDIICE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  96 CAFSHQGSIQVDRNSQsYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGrWTHRAC-QLAHQHTDQVIQLRKAQLQKEG 174
Cdd:cd20660  117 TAMGKSVNAQQNSDSE-YVKAVYRMSELVQKRQKNPWLWPDFIYSLTPDG-REHKKClKILHGFTNKVIQERKAELQKSL 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 175 ELEK-------IKRKGHLDFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 247
Cdd:cd20660  195 EEEEeddedadIGKRKRLAFLDLLLEAS-EEGTKLSDEDIREEVDTFMFEGHDTTAAAINWALYLIGSHPEVQEKVHEEL 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 248 HSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV 326
Cdd:cd20660  274 DRIFGDSdRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDIEI-GGYTIPKGTTVLVLTYALHRDPRQFPDPEK 352

                        330       340
                 ....*....|....*....|....*..
gi 194390028 327 FDPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd20660  353 FDPDRFLPENSAgrHPYAYIPFSAGPR 379
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
 14-351 3.27e-83

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: 258.28  E-value: 3.27e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  14 GSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELlGQDSPLEVFQHVSLMTLDTI 93
Cdd:cd20620   37 GVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEAG-ARRGPVDVHAEMMRLTLRIV 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  94 MKCAFShqgsIQVDRNSQSYIQAISDLNNLVFSRVRNAFHqndtiySLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKE 173
Cdd:cd20620  116 AKTLFG----TDVEGEADEIGDALDVALEYAARRMLSPFL------LPLWLPTPANRRFRRARRRLDEVIYRLIAERRAA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 174 GElekikrkGHLDFLDILLLA-KMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG 252
Cdd:cd20620  186 PA-------DGGDLLSMLLAArDEETGEPMSDQQLRDEVMTLFLAGHETTANALSWTWYLLAQHPEVAARLRAEVDRVLG 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 253 DGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20620  259 GRP-PTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYR-IPAGSTVLISPYVTHRDPRFWPDPEAFDPERF 336

                        330       340
                 ....*....|....*....|.
gi 194390028 333 APGSAQ--HSHAFLPFSGGSR 351
Cdd:cd20620  337 TPEREAarPRYAYFPFGGGPR 357
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
 1-351 4.48e-77

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: 243.51  E-value: 4.48e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSD--PKSHgSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDsP 78
Cdd:cd20680   33 VEVILSSSKhiDKSY-LYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQSNILVEKLEKHVDGE-A 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  79 LEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQsYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQH 158
Cdd:cd20680  111 FNCFFDITLCALDIICETAMGKKIGAQSNKDSE-YVQAVYRMSDIIQRRQKMPWLWLDLWYLMFKEGKEHNKNLKILHTF 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 159 TDQVIQLRKAQLQKE--------GELE-KIKRKGhldFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWI 229
Cdd:cd20680  190 TDNVIAERAEEMKAEedktgdsdGESPsKKKRKA---FLDMLLSVTDEEGNKLSHEDIREEVDTFMFEGHDTTAAAMNWS 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 230 LYALATHPKHQERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVL 308
Cdd:cd20680  267 LYLLGSHPEVQRKVHKELDEVFGKSdRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDCEI-RGFKVPKGVNAV 345

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194390028 309 LSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd20680  346 IIPYALHRDPRYFPEPEEFRPERFFPENSSgrHPYAYIPFSAGPR 390
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
 1-351 7.95e-77

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: 242.51  E-value: 7.95e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSDPKSHGS-YRFLapWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDsPL 79
Cdd:cd11057   22 VQVVLNSPHCLNKSFfYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQKLVQRLDTYVGGG-EF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  80 EVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSqSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHT 159
Cdd:cd11057   99 DILPDLSRCTLEMICQTTLGSDVNDESDGNE-EYLESYERLFELIAKRVLNPWLHPEFIYRLTGDYKEEQKARKILRAFS 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 160 DQVIQLRKAQLQKEGEL----EKIKRKGHLDFLDiLLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALAT 235
Cdd:cd11057  178 EKIIEKKLQEVELESNLdseeDEENGRKPQIFID-QLLELARNGEEFTDEEIMDEIDTMIFAGNDTSATTVAYTLLLLAM 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 236 HPKHQERCREEIHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGL 314
Cdd:cd11057  257 HPEVQEKVYEEIMEVFPDdGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNGVVIPKGTTIVIDIFNM 336

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 194390028 315 HHNPKVW-PNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd11057  337 HRRKDIWgPDADQFDPDNFLPERSAqrHPYAFIPFSAGPR 376
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
 17-351 9.93e-73

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: 230.86  E-value: 9.93e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  17 RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDspLEVFQHVSLMTLDTIMKC 96
Cdd:cd00302   41 PALGDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIREIARELLDRLAAGGEVG--DDVADLAQPLALDVIARL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  97 AFSHQGSIQVDRnsqsYIQAISDLNNLVFSRVRNAFhqndtiysLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQkegel 176
Cdd:cd00302  119 LGGPDLGEDLEE----LAELLEALLKLLGPRLLRPL--------PSPRLRRLRRARARLRDYLEELIARRRAEPA----- 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 177 ekikrkghlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGas 256
Cdd:cd00302  182 ---------DDLDLLLLADADDGGGLSDEEIVAELLTLLLAGHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG-- 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 257 iTWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGS 336
Cdd:cd00302  251 -TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVEL-GGYTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPER 328

                        330
                 ....*....|....*
gi 194390028 337 AQHSHAFLPFSGGSR 351
Cdd:cd00302  329 EEPRYAHLPFGAGPH 343
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
 19-351 6.72e-68

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: 218.99  E-value: 6.72e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  19 LAPWIG-YGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeellGQDSPLEVFQHVSLMTLDTIMKCA 97
Cdd:cd11053   54 LEPLLGpNSLLLLDGDRHRRRRKLLMPAFHGERLRAYGELIAEITEREIDRW----PPGQPFDLRELMQEITLEVILRVV 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  98 FSHQGSIQVDRNSQSYIQAIsDLNNLVFSRVRNAFHQNdtiysltsaGRWT-----HRACQLAHQHTDQVIQLRKAQLQK 172
Cdd:cd11053  130 FGVDDGERLQELRRLLPRLL-DLLSSPLASFPALQRDL---------GPWSpwgrfLRARRRIDALIYAEIAERRAEPDA 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 173 EGElekikrkghlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG 252
Cdd:cd11053  200 ERD----------DILSLLLSARDEDGQPLSDEELRDELMTLLFAGHETTATALAWAFYWLHRHPEVLARLLAELDALGG 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 253 DGASitwNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd11053  270 DPDP---EDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVEL-GGYTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERF 345

                        330
                 ....*....|....*....
gi 194390028 333 ApGSAQHSHAFLPFSGGSR 351
Cdd:cd11053  346 L-GRKPSPYEYLPFGGGVR 363
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
 26-351 7.40e-68

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: 218.99  E-value: 7.40e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  26 GLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQ 105
Cdd:cd11055   51 SLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQ 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 106 VDRNSQSYIQAisdlnnlvfsrvRNAFHQNDTIYSLTSA-----------GRWTHRAcQLAH---QHTDQVIQLRKAQLQ 171
Cdd:cd11055  131 NNPDDPFLKAA------------KKIFRNSIIRLFLLLLlfplrlflfllFPFVFGF-KSFSfleDVVKKIIEQRRKNKS 197

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 172 KEgelekikrkgHLDFLDILLLAK----MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 247
Cdd:cd11055  198 SR----------RKDLLQLMLDAQdsdeDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEI 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 248 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVF 327
Cdd:cd11055  268 DEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWPDPEKF 346

                        330       340
                 ....*....|....*....|....*.
gi 194390028 328 DPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd11055  347 DPERFSPENKAkrHPYAYLPFGAGPR 372
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
 4-351 4.39e-63

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: 207.12  E-value: 4.39e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   4 ILGRSD---PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELL----GQD 76
Cdd:cd11069   27 ILVTNSydfEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAEELVDKLEEEIeesgDES 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  77 SPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQvdRNSQSYIQAISDL-----NNLVFSRVRNAFHQNDTIYSLTSAGRWTHR 150
Cdd:cd11069  107 ISIDVLEWLSRATLDIIGLAGFGYDfDSLE--NPDNELAEAYRRLfeptlLGSLLFILLLFLPRWLVRILPWKANREIRR 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 151 ACQLAHQHTDQVIQLRKAQLQKEGELEKikrkghLDFLDILLLAKME-NGSILSDKDLRAEVDTFMFEGHDTTASGISWI 229
Cdd:cd11069  185 AKDVLRRLAREIIREKKAALLEGKDDSG------KDILSILLRANDFaDDERLSDEELIDQILTFLAAGHETTSTALTWA 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 230 LYALATHPKHQERCREEIHSLLGD--GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPvTFPDGRSLPKGIMV 307
Cdd:cd11069  259 LYLLAKHPDVQERLREEIRAALPDppDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREATKD-TVIKGVPIPKGTVV 337

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194390028 308 LLSIYGLHHNPKVW-PNPEVFDPFRF-------APGSAQHSHAFLPFSGGSR 351
Cdd:cd11069  338 LIPPAAINRSPEIWgPDAEEFNPERWlepdgaaSPGGAGSNYALLTFLHGPR 389
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
 27-351 1.57e-59

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: 197.38  E-value: 1.57e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  27 LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFShqgsiqV 106
Cdd:cd11056   53 LFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFG------L 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 107 DRNSqsyiqaISDLNNLVFSRVRNAFHQNDTIY----SLTSAGRWTH--RACQLAHQHTD-------QVIQLRkaqlqke 173
Cdd:cd11056  127 DANS------LNDPENEFREMGRRLFEPSRLRGlkfmLLFFFPKLARllRLKFFPKEVEDffrklvrDTIEYR------- 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 174 gELEKIKRKghlDFLDILL-------LAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE 246
Cdd:cd11056  194 -EKNNIVRN---DFIDLLLelkkkgkIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREE 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 247 IHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNP 324
Cdd:cd11056  270 IDEVLEKhGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvVIEKGTPVIIPVYALHHDPKYYPEP 349

                        330       340
                 ....*....|....*....|....*....
gi 194390028 325 EVFDPFRFAPG--SAQHSHAFLPFSGGSR 351
Cdd:cd11056  350 EKFDPERFSPEnkKKRHPYTYLPFGDGPR 378
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
 2-351 3.07e-58

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: 194.10  E-value: 3.07e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   2 KVILGRSDPKSHGSY--RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLG-QDSP 78
Cdd:cd11052   34 KELLSKKEGYFGKSPlqPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHGEKLKGMVPAMVESVSDMLERWKKQMGeEGEE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  79 LEVFQHVSLMTLDTIMKCAF--SHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIysltsagrwthRACQLAH 156
Cdd:cd11052  114 VDVFEEFKALTADIISRTAFgsSYEEGKEVFKLLRELQKICAQANRDVGIPGSRFLPTKGNK-----------KIKKLDK 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 157 QHTDQVIQLRKAQLQKEGELEKiKRKGHlDFLDILLLA--KMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALA 234
Cdd:cd11052  183 EIEDSLLEIIKKREDSLKMGRG-DDYGD-DLLGLLLEAnqSDDQNKNMTVQEIVDECKTFFFAGHETTALLLTWTTMLLA 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 235 THPKHQERCREEIHSLLGDGaSITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGL 314
Cdd:cd11052  261 IHPEWQEKAREEVLEVCGKD-KPPSDSLSKLKTVSMVINESLRLYPPAVFLTRKAKEDIKL-GGLVIPKGTSIWIPVLAL 338

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 194390028 315 HHNPKVWPN-PEVFDPFRFAPGSAQ---HSHAFLPFSGGSR 351
Cdd:cd11052  339 HHDEEIWGEdANEFNPERFADGVAKaakHPMAFLPFGLGPR 379
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
 2-351 1.21e-57

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: 192.96  E-value: 1.21e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   2 KVILgRSDPKSHGSYRFLA----PWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDS 77
Cdd:cd11046   33 KHVL-RSNAFSYDKKGLLAeilePIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRCSERLMEKLDAAAETGE 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  78 PLEVFQHVSLMTLDTIMKCAFSHQ-GSIQvdrNSQSYIQAisdlnnlVFSRVRNAFHQN-------DTIYSLTSAGRWTH 149
Cdd:cd11046  112 SVDMEEEFSSLTLDIIGLAVFNYDfGSVT---EESPVIKA-------VYLPLVEAEHRSvweppywDIPAALFIVPRQRK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 150 --RACQLAHQHTDQVIQLRKAQLQKEG-ELEKIKRKGHLDFLDILLLAKMeNGSILSDKDLRAEVDTFMFEGHDTTASGI 226
Cdd:cd11046  182 flRDLKLLNDTLDDLIRKRKEMRQEEDiELQQEDYLNEDDPSLLRFLVDM-RDEDVDSKQLRDDLMTMLIAGHETTAAVL 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 227 SWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGI 305
Cdd:cd11046  261 TWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVEDDKLPGGGvKVPAGT 340

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194390028 306 MVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH------AFLPFSGGSR 351
Cdd:cd11046  341 DIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNeviddfAFLPFGGGPR 392
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
 10-351 7.75e-56

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: 187.73  E-value: 7.75e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  10 PKSHGSYRFLA-----PWIGYGLL-LLNGQTWFQHRRMLTPAFHYDILKpyvGLMA---DSVRVMLDKWEELlgQDSPLE 80
Cdd:cd20613   43 PKPPRVYSRLAflfgeRFLGNGLVtEVDHEKWKKRRAILNPAFHRKYLK---NLMDefnESADLLVEKLSKK--ADGKTE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  81 V--FQHVSLMTLDTIMKCAFSHQGSIQVDRNSQsYIQAISD-LNNLVFSRvRNAFHQndtiyslTSAGRWTHR-----AC 152
Cdd:cd20613  118 VnmLDEFNRVTLDVIAKVAFGMDLNSIEDPDSP-FPKAISLvLEGIQESF-RNPLLK-------YNPSKRKYRrevreAI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 153 QLAHQHTDQVIQLRKAQLQKEGELEKikrkghldflDIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWIL 230
Cdd:cd20613  189 KFLRETGRECIEERLEALKRGEEVPN----------DILthILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTL 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 231 YALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLS 310
Cdd:cd20613  259 LELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQVLKETLRLYPPVPGTSRELTKDIEL-GGYKIPAGTTVLVS 337

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 194390028 311 IYGLHHNPKVWPNPEVFDPFRFAPGS--AQHSHAFLPFSGGSR 351
Cdd:cd20613  338 TYVMGRMEEYFEDPLKFDPERFSPEApeKIPSYAYFPFSLGPR 380
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
 16-351 2.30e-54

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: 183.61  E-value: 2.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  16 YRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllGQdsPLEVFQHVSLMTLDTIMK 95
Cdd:cd11049   51 FDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWRP--GR--VVDVDAEMHRLTLRVVAR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  96 CAFSHQGSiqvDRNSQSYIQAISDLNNLVFSRvrnafhqndTIY--SL----TSAGRWTHRACQLAHQHTDQVIQLRKAQ 169
Cdd:cd11049  127 TLFSTDLG---PEAAAELRQALPVVLAGMLRR---------AVPpkFLerlpTPGNRRFDRALARLRELVDEIIAEYRAS 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 170 LQKEGelekikrkghlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHS 249
Cdd:cd11049  195 GTDRD-----------DLLSLLLAARDEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDA 263

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 250 LLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDP 329
Cdd:cd11049  264 VLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVEL-GGHRLPAGTEVAFSPYALHRDPEVYPDPERFDP 341

                        330       340
                 ....*....|....*....|....
gi 194390028 330 FRFAPG--SAQHSHAFLPFSGGSR 351
Cdd:cd11049  342 DRWLPGraAAVPRGAFIPFGAGAR 365
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
 11-351 5.28e-52

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


Pssm-ID: 441727 [Multi-domain]  Cd Length: 400  Bit Score: 177.01  E-value: 5.28e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  11 KSHGSYRFLAP--WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllgqDSPLEVFQHVSLM 88
Cdd:COG2124   65 SDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRIREIADELLDRLAA----RGPVDLVEEFARP 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  89 TLDTIMKCAFSHQGSiqvDRNSqsyiqaisdlnnlvFSRVRNAFHQNDTIYSLTSAGRwTHRACQLAHQHTDQVIQLRKA 168
Cdd:COG2124  141 LPVIVICELLGVPEE---DRDR--------------LRRWSDALLDALGPLPPERRRR-ARRARAELDAYLRELIAERRA 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 169 QLQKegelekikrkghlDFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIh 248
Cdd:COG2124  203 EPGD-------------DLLSALLAAR-DDGERLSDEELRDELLLLLLAGHETTANALAWALYALLRHPEQLARLRAEP- 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 249 sllgdgasitwnhldqmPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFD 328
Cdd:COG2124  268 -----------------ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GGVTIPAGDRVLLSLAAANRDPRVFPDPDRFD 329

                        330       340
                 ....*....|....*....|...
gi 194390028 329 PFRfapgsaqHSHAFLPFSGGSR 351
Cdd:COG2124  330 PDR-------PPNAHLPFGGGPH 345
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
 25-351 2.77e-51

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: 175.79  E-value: 2.77e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  25 YGLLLLNGQTWFQHRRMLTPafhyDILKP-----YVGLMADSVRVMLDKWEELLGQDS--PLEVFQHVSLMTLDTIMKCA 97
Cdd:cd11054   56 LGLLNSNGEEWHRLRSAVQK----PLLRPksvasYLPAINEVADDFVERIRRLRDEDGeeVPDLEDELYKWSLESIGTVL 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  98 F-SHQGSIQVDRNS--QSYIQAISDLNNLVfsrvrnafhqNDTIYSLTSAGRW-THRACQLAhQHTDQVIQLRKAQLQKE 173
Cdd:cd11054  132 FgKRLGCLDDNPDSdaQKLIEAVKDIFESS----------AKLMFGPPLWKYFpTPAWKKFV-KAWDTIFDIASKYVDEA 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 174 geLEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGD 253
Cdd:cd11054  201 --LEELKKKDEEDEEEDSLLEYLLSKPGLSKKEIVTMALDLLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPD 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 254 GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF- 332
Cdd:cd11054  279 GEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDIVL-SGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWl 357

                        330       340
                 ....*....|....*....|..
gi 194390028 333 ---APGSAQHSHAFLPFSGGSR 351
Cdd:cd11054  358 rddSENKNIHPFASLPFGFGPR 379
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
 7-351 2.56e-50

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: 173.52  E-value: 2.56e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   7 RSDPKSHGSYRFLAPWIGYGLLLLNG--QTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELlGQDSPLEVFQH 84
Cdd:cd11068   42 RFDKKVSGPLEELRDFAGDGLFTAYThePNWGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERL-GPDEPIDVPDD 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  85 VSLMTLDTIMKCAFSHQ-GSIQVDRnSQSYIQAISDLNNLVFSRVRNAFHQNDTiysLTSAGRWTHRACQLAHQHTDQVI 163
Cdd:cd11068  121 MTRLTLDTIALCGFGYRfNSFYRDE-PHPFVEAMVRALTEAGRRANRPPILNKL---RRRAKRQFREDIALMRDLVDEII 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 164 QLRKAQlqkegelekiKRKGHLDFLDILLLAK-MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 242
Cdd:cd11068  197 AERRAN----------PDGSPDDLLNLMLNGKdPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAK 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 243 CREEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW- 321
Cdd:cd11068  267 ARAEVDEVLGDDP-PPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWg 345

                        330       340       350
                 ....*....|....*....|....*....|..
gi 194390028 322 PNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSR 351
Cdd:cd11068  346 EDAEEFRPERFLPEEFRklPPNAWKPFGNGQR 377
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
 24-351 5.05e-49

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: 169.70  E-value: 5.05e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  24 GYGLLLLNGQTWFQHRRMLTPAF--HYDILKPYvGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ 101
Cdd:cd20617   48 GKGILFSNGDYWKELRRFALSSLtkTKLKKKME-ELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 102 GSIQVDRNSQSYIQAISDLNNLV-FSRVRNAFHQNDTIYSLTSagRWTHRACQLAHQHTDQVIQLRKAQLQKEGELekik 180
Cdd:cd20617  127 FPDEDDGEFLKLVKPIEEIFKELgSGNPSDFIPILLPFYFLYL--KKLKKSYDKIKDFIEKIIEEHLKTIDPNNPR---- 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 181 rkgHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 260
Cdd:cd20617  201 ---DLIDDELLLLLKEGDSGLFDDDSIISTCLDLFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLS 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 261 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQ 338
Cdd:cd20617  278 DRSKLPYLNAVIKEVLRLRPILPlGLPRVTTEDTEI-GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNK 356

                        330
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd20617  357 LSEQFIPFGIGKR 369
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
 22-351 1.14e-48

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: 169.00  E-value: 1.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  22 WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQ 101
Cdd:cd11044   66 LGENSLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLK----AGEVALYPELRRLTFDVAARLLLGLD 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 102 GSIQVDRNSQSYIQAISDLN----NLVFSRVRNAFhqndtiysltsagrwthRACQLAHQHTDQVIQLRKAQLQKEGele 177
Cdd:cd11044  142 PEVEAEALSQDFETWTDGLFslpvPLPFTPFGRAI-----------------RARNKLLARLEQAIRERQEEENAEA--- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 178 kikrkghLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAsI 257
Cdd:cd11044  202 -------KDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEP-L 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 258 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP-GS 336
Cdd:cd11044  274 TLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPaRS 352

                        330
                 ....*....|....*..
gi 194390028 337 AQHSHAF--LPFSGGSR 351
Cdd:cd11044  353 EDKKKPFslIPFGGGPR 369
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
 36-350 4.76e-48

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: 167.01  E-value: 4.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  36 FQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeellGQDSPLEVFQHVSLMTLDTIMKCAfshQGSiqvdrnsqsyiq 115
Cdd:cd11042   65 KEQLKFGLNILRRGKLRGYVPLIVEEVEKYFAKW----GESGEVDLFEEMSELTILTASRCL---LGK------------ 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 116 aisDLNNLVFSRVRNAFHQNDTIYSLTSAGRW-----THRACQLAHQHTD----QVIQLRKAQLQKEGelekikrkghLD 186
Cdd:cd11042  126 ---EVRELLDDEFAQLYHDLDGGFTPIAFFFPplplpSFRRRDRARAKLKeifsEIIQKRRKSPDKDE----------DD 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 187 FLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGD-GASITWNHLDQM 265
Cdd:cd11042  193 MLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDgDDPLTYDVLKEM 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 266 PYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH--- 341
Cdd:cd11042  273 PLLHACIKETLRLHPPIHSLMRKARKPFEVEGGGyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKggk 352

                        330
                 ....*....|
gi 194390028 342 -AFLPFSGGS 350
Cdd:cd11042  353 fAYLPFGAGR 362
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
 23-351 6.09e-47

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: 164.55  E-value: 6.09e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  23 IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEV-----FQHVslmTLDTIMKCA 97
Cdd:cd20639   57 EGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVVKSVADMLDKWEAMAEAGGEGEVdvaewFQNL---TEDVISRTA 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  98 FshqGSiqvdrnsqSYIQAisdlnnlvfsrvRNAFHQNDTIYSLTSAGRWT--------------HRACQLAHQ---HTD 160
Cdd:cd20639  134 F---GS--------SYEDG------------KAVFRLQAQQMLLAAEAFRKvyipgyrflptkknRKSWRLDKEirkSLL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKrkghlDFLDILLLAK-MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKH 239
Cdd:cd20639  191 KLIERRQTAADDEKDDEDSK-----DLLGLMISAKnARNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEW 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 240 QERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPK 319
Cdd:cd20639  266 QERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETLRLYPPAVATIRRAKKDVKL-GGLDIPAGTELLIPIMAIHHDAE 344

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 194390028 320 VW-PNPEVFDPFRFAPGS---AQHSHAFLPFSGGSR 351
Cdd:cd20639  345 LWgNDAAEFNPARFADGVaraAKHPLAFIPFGLGPR 380
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
 25-351 2.17e-45

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: 160.04  E-value: 2.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  25 YGLLLLNGqtwFQHRRM---LTPAFHYDILKP-YVGLMADSVRVMLDKWEellgqDSPLEVFQ-HVSLMTLDTIMKCAFS 99
Cdd:cd11043   53 SSLLTVSG---EEHKRLrglLLSFLGPEALKDrLLGDIDELVRQHLDSWW-----RGKSVVVLeLAKKMTFELICKLLLG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 100 HQGSIQVDRNSQSYIQAISDLN----NLVFSRVRNAFHqndtiysltsagrwthrACQLAHQHTDQVIQLRKAQLQKEGE 175
Cdd:cd11043  125 IDPEEVVEELRKEFQAFLEGLLsfplNLPGTTFHRALK-----------------ARKRIRKELKKIIEERRAELEKASP 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 176 LEkikrkghlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE---IHSLLG 252
Cdd:cd11043  188 KG--------DLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeIAKRKE 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 253 DGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd11043  260 EGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEY-KGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW 338

                        330
                 ....*....|....*....
gi 194390028 333 APGSAQHSHAFLPFSGGSR 351
Cdd:cd11043  339 EGKGKGVPYTFLPFGGGPR 357
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
 18-349 8.28e-45

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


Pssm-ID: 410671 [Multi-domain]  Cd Length: 407  Bit Score: 158.25  E-value: 8.28e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  18 FLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCA 97
Cdd:cd11045   52 VIGPFFHRGLMLLDFDEHRAHRRIMQQAFTRSALAGYLDRMTPGIERALARWPT----GAGFQFYPAIKELTLDLATRVF 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  98 FSHQGSIQVDRNSQSYIQAISDLNNLVFSRVrnafhqndtiysltSAGRWtHRACQlAHQHTDQVIQLRKAQlQKEGELE 177
Cdd:cd11045  128 LGVDLGPEADKVNKAFIDTVRASTAIIRTPI--------------PGTRW-WRGLR-GRRYLEEYFRRRIPE-RRAGGGD 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 178 kikrkghlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLlGDGAsI 257
Cdd:cd11045  191 --------DLFSALCRAEDEDGDRFSDDDIVNHMIFLMMAAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGT-L 260

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 258 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 337
Cdd:cd11045  261 DYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV-LGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERA 339

                        330
                 ....*....|....*
gi 194390028 338 ---QHSHAFLPFSGG 349
Cdd:cd11045  340 edkVHRYAWAPFGGG 354
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
 19-351 1.92e-42

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: 152.33  E-value: 1.92e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  19 LAPWIGYGLLLLNGQTWFQHRRMLTPAF------HYDILKPYVGLMADSVRvmldkweellGQDSPLEVFQHVSLMTLDT 92
Cdd:cd11063   44 FKPLLGDGIFTSDGEEWKHSRALLRPQFsrdqisDLELFERHVQNLIKLLP----------RDGSTVDLQDLFFRLTLDS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  93 IMKCAFSHqgSIQVDRNSQSYI------QAISDLNNLVFSRVRNafhqnDTIYSLTSAGRWtHRACQLAHQHTDQVIQlr 166
Cdd:cd11063  114 ATEFLFGE--SVDSLKPGGDSPpaarfaEAFDYAQKYLAKRLRL-----GKLLWLLRDKKF-REACKVVHRFVDPYVD-- 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 167 KAQLQKEGELEKiKRKGHLDFLDilLLAKmengSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE 246
Cdd:cd11063  184 KALARKEESKDE-ESSDRYVFLD--ELAK----ETRDPKELRDQLLNILLAGRDTTASLLSFLFYELARHPEVWAKLREE 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 247 IHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFP-----DGRS---LPKGIMVLLSIYGLHHNP 318
Cdd:cd11063  257 VLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLPrgggpDGKSpifVPKGTRVLYSVYAMHRRK 336

                        330       340       350
                 ....*....|....*....|....*....|....
gi 194390028 319 KVW-PNPEVFDPFRFAPGSaQHSHAFLPFSGGSR 351
Cdd:cd11063  337 DIWgPDAEEFRPERWEDLK-RPGWEYLPFNGGPR 369
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
 10-351 2.63e-42

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: 152.48  E-value: 2.63e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  10 PKSHGSYRFLAPwigYG--LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEE--LLGQDSPLEVFQHV 85
Cdd:cd11070   34 PKPGNQYKIPAF---YGpnVISSEGEDWKRYRKIVAPAFNERNNALVWEESIRQAQRLIRYLLEeqPSAKGGGVDVRDLL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  86 SLMTLDTIMKCAFSHQGSIQvDRNSQSYIQAISDLNNLVFSRVRNAFhqndTIYSLTsaGRWTHRACQLAHQhtdQVIQL 165
Cdd:cd11070  111 QRLALNVIGEVGFGFDLPAL-DEEESSLHDTLNAIKLAIFPPLFLNF----PFLDRL--PWVLFPSRKRAFK---DVDEF 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 166 RKAqLQKEGELEKIKRKGHLDFLDILL---LAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 242
Cdd:cd11070  181 LSE-LLDEVEAELSADSKGKQGTESVVasrLKRARRSGGLTEKELLGNLFIFFIAGHETTANTLSFALYLLAKHPEVQDW 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 243 CREEIHSLLGDGASITWNH--LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRS----LPKGIMVLLSIYGLHH 316
Cdd:cd11070  260 LREEIDSVLGDEPDDWDYEedFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGLGqeivIPKGTYVGYNAYATHR 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 194390028 317 NPKVW-PNPEVFDPFRFAPGS-----AQHSH----AFLPFSGGSR 351
Cdd:cd11070  340 DPTIWgPDADEFDPERWGSTSgeigaATRFTpargAFIPFSAGPR 384
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
 23-351 3.47e-42

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: 151.83  E-value: 3.47e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  23 IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSL----MTLDTIMKCAF 98
Cdd:cd20641   57 SGKGLVFVNGDDWVRHRRVLNPAFSMDKLKSMTQVMADCTERMFQEWRKQRNNSETERIEVEVSRefqdLTADIIATTAF 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  99 --SHQGSIQVDRnSQSYIQ--AISDLNNLVFSrvrnafhqnDTIYSLTSAGRwthRACQLAHQHTDQVIQLRKAQLQKEG 174
Cdd:cd20641  137 gsSYAEGIEVFL-SQLELQkcAAASLTNLYIP---------GTQYLPTPRNL---RVWKLEKKVRNSIKRIIDSRLTSEG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 175 elekikrKGH-LDFLDILLLAKMENGS------ILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 247
Cdd:cd20641  204 -------KGYgDDLLGLMLEAASSNEGgrrterKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEV 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 248 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEV 326
Cdd:cd20641  277 FRECGKDKIPDADTLSKLKLMNMVLMETLRLYGPVINIARRASEDMKL-GGLEIPKGTTIIIPIAKLHRDKEVWgSDADE 355

                        330       340
                 ....*....|....*....|....*...
gi 194390028 327 FDPFRFAPG---SAQHSHAFLPFSGGSR 351
Cdd:cd20641  356 FNPLRFANGvsrAATHPNALLSFSLGPR 383
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
 23-351 8.10e-42

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: 150.87  E-value: 8.10e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  23 IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQdspleVFQHVSLMTLDTIMKCAFS--- 99
Cdd:cd20621   47 FGKGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEITKEKIKKLDNQNVN-----IIQFLQKITGEVVIRSFFGeea 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 100 -----HQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEg 174
Cdd:cd20621  122 kdlkiNGKEIQVELVEILIESFLYRFSSPYFQLKRLIFGRKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKN- 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 175 eleKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG 254
Cdd:cd20621  201 ---KDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFITFFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGND 277

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 255 ASITWNHLDQMPYTTMCIKEALRLYPPVPG-IGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF- 332
Cdd:cd20621  278 DDITFEDLQKLNYLNAFIKEVLRLYNPAPFlFPRVATQDHQIGD-LKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWl 356

                        330       340
                 ....*....|....*....|
gi 194390028 333 -APGSAQHSHAFLPFSGGSR 351
Cdd:cd20621  357 nQNNIEDNPFVFIPFSAGPR 376
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
 19-351 8.97e-42

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: 150.64  E-value: 8.97e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  19 LAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELL----GQDSPLEVFQHVSLMTLDTIM 94
Cdd:cd20640   54 LKPLFGGGILTSNGPHWAHQRKIIAPEFFLDKVKGMVDLMVDSAQPLLSSWEERIdragGMAADIVVDEDLRAFSADVIS 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  95 KCAFshqGSiqvdrnsqSYIQAISdlnnlVFSRVRN---AFHQNDTIYSLTSAgRWTHRACQLAHQHTDQVIQLRKAQLQ 171
Cdd:cd20640  134 RACF---GS--------SYSKGKE-----IFSKLRElqkAVSKQSVLFSIPGL-RHLPTKSNRKIWELEGEIRSLILEIV 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 172 KEGELEKIKRKghlDFLDILLLAKMengsilSDKDLRAEVDTFM--------FEGHDTTASGISWILYALATHPKHQERC 243
Cdd:cd20640  197 KEREEECDHEK---DLLQAILEGAR------SSCDKKAEAEDFIvdnckniyFAGHETTAVTAAWCLMLLALHPEWQDRV 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 244 REEIHSLLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVW-P 322
Cdd:cd20640  268 RAEVLEVCK-GGPPDADSLSRMKTVTMVIQETLRLYPPAAFVSREALRDMKLGGLV-VPKGVNIWVPVSTLHLDPEIWgP 345

                        330       340       350
                 ....*....|....*....|....*....|..
gi 194390028 323 NPEVFDPFRFA---PGSAQHSHAFLPFSGGSR 351
Cdd:cd20640  346 DANEFNPERFSngvAAACKPPHSYMPFGAGAR 377
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
 1-351 4.04e-41

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: 148.99  E-value: 4.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   1 MKVILGRSDPKSHG-SYRFLAPWIGYGLL-LLNGQTWFQHRRMLTPAFHydilKPYVGL------MADSVRVMLDKWEEL 72
Cdd:cd11059   19 VREIYGGGFGKTKSyWYFTLRGGGGPNLFsTLDPKEHSARRRLLSGVYS----KSSLLRaamepiIRERVLPLIDRIAKE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  73 LGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYiqaisdlnnlvfSRVRNAFHQNDTIYSLTSAGRWTHRA- 151
Cdd:cd11059   95 AGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSR------------ERELLRRLLASLAPWLRWLPRYLPLAt 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 152 -------CQLAHQHTDQ-VIQLRKAQLQKEGELEKIKRKGHLDFLDilllAKMENGSILSDKDLRAEVDTFMFEGHDTTA 223
Cdd:cd11059  163 srliigiYFRAFDEIEEwALDLCARAESSLAESSDSESLTVLLLEK----LKGLKKQGLDDLEIASEALDHIVAGHDTTA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 224 SGISWILYALATHPKHQERCREEIHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIG-RELSTPVTFPDGRSL 301
Cdd:cd11059  239 VTLTYLIWELSRPPNLQEKLREELAGLPGPfRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLpRVVPEGGATIGGYYI 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194390028 302 PKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH----AFLPFSGGSR 351
Cdd:cd11059  319 PGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETARemkrAFWPFGSGSR 372
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
 8-351 8.41e-41

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: 147.40  E-value: 8.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   8 SDPKSHGSYRFLAPWIG-YGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVS 86
Cdd:cd11051   29 NLPKPPPLRKFLTPLTGgSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAILRELAESGEVFSLEELTT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  87 LMTLDTIMKCAFShqgsiqVDRNSQSYIQAISDLNNLVFSRVRNAFHqndtIYSLTSAGRWTHRAcQLAHQhTDQVIQlr 166
Cdd:cd11051  109 NLTFDVIGRVTLD------IDLHAQTGDNSLLTALRLLLALYRSLLN----PFKRLNPLRPLRRW-RNGRR-LDRYLK-- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 167 kaqlqkegelEKIKRKGHLDFLdilllakmengsilsdkdlRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE 246
Cdd:cd11051  175 ----------PEVRKRFELERA-------------------IDQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVRAE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 247 IHSLLGDGASITW-------NHLDQMPYTTMCIKEALRLYPPV-------PGIGrelstpVTFPDGRSLP-KGIMVLLSI 311
Cdd:cd11051  226 HDEVFGPDPSAAAellregpELLNQLPYTTAVIKETLRLFPPAgtarrgpPGVG------LTDRDGKEYPtDGCIVYVCH 299

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 194390028 312 YGLHHNPKVWPNPEVFDPFRF--APGSAQH--SHAFLPFSGGSR 351
Cdd:cd11051  300 HAIHRDPEYWPRPDEFIPERWlvDEGHELYppKSAWRPFERGPR 343
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
 24-351 6.83e-40

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: 145.81  E-value: 6.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  24 GYGLLLLNGQTWFQHRRMLTPAFHydiLKPYVGLMADSVRvmlDKWEELL--------GQDSPLEvFQHVSL-MTLDTIM 94
Cdd:cd11064   48 GDGIFNVDGELWKFQRKTASHEFS---SRALREFMESVVR---EKVEKLLvplldhaaESGKVVD-LQDVLQrFTFDVIC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  95 KCAFSHQ-GSIQVDRNSQSYIQAISDLNNLVFSRvrnaFHQNDTIYSLTsagRWTH--------RACQLAHQHTDQVIQL 165
Cdd:cd11064  121 KIAFGVDpGSLSPSLPEVPFAKAFDDASEAVAKR----FIVPPWLWKLK---RWLNigsekklrEAIRVIDDFVYEVISR 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 166 RKAQLQKEGElekiKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCRE 245
Cdd:cd11064  194 RREELNSREE----ENNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIRE 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 246 EIHSLLGDGASITW-----NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKV 320
Cdd:cd11064  270 ELKSKLPKLTTDESrvptyEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESI 349

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 194390028 321 W-PNPEVFDPFRF--APGSAQH--SHAFLPFSGGSR 351
Cdd:cd11064  350 WgEDALEFKPERWldEDGGLRPesPYKFPAFNAGPR 385
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
 177-351 3.51e-36

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: 135.62  E-value: 3.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 177 EKIKRKGHLDFLDILLLAKMENGS----ILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG 252
Cdd:cd20650  195 LDSTQKHRVDFLQLMIDSQNSKETeshkALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLP 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 253 DGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20650  275 NKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEI-NGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF 353

                        170       180
                 ....*....|....*....|.
gi 194390028 333 APGSAQH--SHAFLPFSGGSR 351
Cdd:cd20650  354 SKKNKDNidPYIYLPFGSGPR 374
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 32-351 7.48e-36

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: 134.64  E-value: 7.48e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  32 GQTWFQHRRMLTPAFHY--DILKPYVGLMADSVRVMLDKWEELLGQdsPLEVFQHVSLMTLDTImkCAFSHQGSIQVDRN 109
Cdd:cd11027   59 SPTWKLHRKLAHSALRLyaSGGPRLEEKIAEEAEKLLKRLASQEGQ--PFDPKDELFLAVLNVI--CSITFGKRYKLDDP 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 110 SqsyIQAISDLNNlVFSRVRNAFHQNDTIYSLtsagRW----THRACQLAHQHTDQVIQlRKAQLQKEGELEKIKRkghl 185
Cdd:cd11027  135 E---FLRLLDLND-KFFELLGAGSLLDIFPFL----KYfpnkALRELKELMKERDEILR-KKLEEHKETFDPGNIR---- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKME-------NGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT 258
Cdd:cd11027  202 DLTDALIKAKKEaedegdeDSGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPT 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 259 WNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 337
Cdd:cd11027  282 LSDRKRLPYLEATIAEVLRLSSVVPlALPHKTTCDTTL-RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENG 360

                        330
                 ....*....|....*..
gi 194390028 338 Q---HSHAFLPFSGGSR 351
Cdd:cd11027  361 KlvpKPESFLPFSAGRR 377
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
 10-351 3.14e-35

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: 133.17  E-value: 3.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  10 PKSHgsYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQD--SPLEVFQHVSL 87
Cdd:cd20642   44 QKPK--TNPLTKLLATGLASYEGDKWAKHRKIINPAFHLEKLKNMLPAFYLSCSEMISKWEKLVSSKgsCELDVWPELQN 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  88 MTLDTIMKCAFshqGSiqvdrnsqSYIQAISdlnnlVFSRVRN-AFHQNDTIYSLTSAGRW-----THRACQLAHQhtdQ 161
Cdd:cd20642  122 LTSDVISRTAF---GS--------SYEEGKK-----IFELQKEqGELIIQALRKVYIPGWRflptkRNRRMKEIEK---E 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 162 VIQLRKAQLQKEGELEKIKRKGHLDFLDILLLA------KMENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALA 234
Cdd:cd20642  183 IRSSLRGIINKREKAMKAGEATNDDLLGILLESnhkeikEQGNKNGgMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLS 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 235 THPKHQERCREEIHSLLGDGASiTWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDgRSLPKGIMVLLSIYGL 314
Cdd:cd20642  263 QHPDWQERAREEVLQVFGNNKP-DFEGLNHLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGD-LTLPAGVQVSLPILLV 340

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 194390028 315 HHNPKVWPN-PEVFDPFRFAPGSAQHSH---AFLPFSGGSR 351
Cdd:cd20642  341 HRDPELWGDdAKEFNPERFAEGISKATKgqvSYFPFGWGPR 381
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
 27-332 9.15e-35

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: 131.93  E-value: 9.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  27 LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLdkwEELLgqDSPLEVFQHVSLMTLDTIMKCAFshqGsIQV 106
Cdd:cd11065   54 LLMPYGPRWRLHRRLFHQLLNPSAVRKYRPLQELESKQLL---RDLL--ESPDDFLDHIRRYAASIILRLAY---G-YRV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 107 DRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTS------------AGRWTHRACQLAHQHTDQViqlrkaqlqkeg 174
Cdd:cd11065  125 PSYDDPLLRDAEEAMEGFSEAGSPGAYLVDFFPFLRYlpswlgapwkrkARELRELTRRLYEGPFEAA------------ 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 175 eLEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG 254
Cdd:cd11065  193 -KERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPD 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194390028 255 ASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd11065  272 RLPTFEDRPNLPYVNAIVKEVLRWRPVAPlGIPHALTEDDEY-EGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERY 349
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 37-351 9.60e-35

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: 131.55  E-value: 9.60e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  37 QHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQVDRNSQSYIQ 115
Cdd:cd11060   59 ALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLDEKAVSGKEVDLGKWLQYFAFDVIGEITFGKPfGFLEAGTDVDGYIA 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 116 AIsDLNNLVFSRV------RNAFHQNDTIYSLTSAGRWTHracqlahqhtdqVIQLRKAQLQKEGELEKIKRKGHLDFLD 189
Cdd:cd11060  139 SI-DKLLPYFAVVgqipwlDRLLLKNPLGPKRKDKTGFGP------------LMRFALEAVAERLAEDAESAKGRKDMLD 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 190 ILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAS---ITWNHLDQMP 266
Cdd:cd11060  206 SFLEAGLKDPEKVTDREVVAEALSNILAGSDTTAIALRAILYYLLKNPRVYAKLRAEIDAAVAEGKLsspITFAEAQKLP 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 267 YTTMCIKEALRLYPPVpGIGRELSTP---VTFPdGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF--APGS--AQ 338
Cdd:cd11060  286 YLQAVIKEALRLHPPV-GLPLERVVPpggATIC-GRFIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEEqrRM 363

                        330
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd11060  364 MDRADLTFGAGSR 376
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
 37-351 1.23e-34

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: 131.19  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  37 QHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDS--PLEVFQHVSLMTLDTIMKCAFSHQ-GSIqvDRNSQSY 113
Cdd:cd11061   56 RRRRVWSHAFSDKALRGYEPRILSHVEQLCEQLDDRAGKPVswPVDMSDWFNYLSFDVMGDLAFGKSfGML--ESGKDRY 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 114 IQAISDLNNLVFSRVRNAfhqnDTIYSLTSAGRWTHRAcqlaHQHTDQVIQLRKAQLQKEGELEKIKRKghlDFLDILLL 193
Cdd:cd11061  134 ILDLLEKSMVRLGVLGHA----PWLRPLLLDLPLFPGA----TKARKRFLDFVRAQLKERLKAEEEKRP---DIFSYLLE 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 194 AKM-ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASI-TWNHLDQMPYTTMC 271
Cdd:cd11061  203 AKDpETGEGLDLEELVGEARLLIVAGSDTTATALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIrLGPKLKSLPYLRAC 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 272 IKEALRLYPPVPGIG-RElsTP---VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH---AFL 344
Cdd:cd11061  283 IDEALRLSPPVPSGLpRE--TPpggLTI-DGEYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRarsAFI 359


                 ....*..
gi 194390028 345 PFSGGSR 351
Cdd:cd11061  360 PFSIGPR 366
PLN02290 PLN02290
cytokinin trans-hydroxylase
 6-351 1.49e-34

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 132.63  E-value: 1.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   6 GRSDPKSHGSYRFlapwIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQ-DSPLEVFQH 84
Cdd:PLN02290 127 GKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESgQTEVEIGEY 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  85 VSLMTLDTIMKCAFSHQgsiqVDRNSQSYiQAISDLNNLVFSRVRNAF---------HQNDTIYSLTSagrwthracqla 155
Cdd:PLN02290 203 MTRLTADIISRTEFDSS----YEKGKQIF-HLLTVLQRLCAQATRHLCfpgsrffpsKYNREIKSLKG------------ 265

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 156 hqhtdQVIQLRKAQLQKEGELEKIKR-KGHLDFLDILLLAKME----NGSILSDKDLRAEVDTFMFEGHDTTASGISWIL 230
Cdd:PLN02290 266 -----EVERLLMEIIQSRRDCVEIGRsSSYGDDLLGMLLNEMEkkrsNGFNLNLQLIMDECKTFFFAGHETTALLLTWTL 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 231 YALATHPKHQERCREEIHSLLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLS 310
Cdd:PLN02290 341 MLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIP 418

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 194390028 311 IYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGSR 351
Cdd:PLN02290 419 VLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFIPFAAGPR 460
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
 26-351 4.01e-34

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: 130.13  E-value: 4.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  26 GLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSI 104
Cdd:cd11083   50 GVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDlNTL 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 105 QVDRNsqsyiqAISDLNNLVF----SRVRNAFHQNDtiYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIK 180
Cdd:cd11083  130 ERGGD------PLQEHLERVFpmlnRRVNAPFPYWR--YLRLPADRALDRALVEVRALVLDIIAAARARLAANPALAEAP 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 181 RKghldfLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT-W 259
Cdd:cd11083  202 ET-----LLAMMLAEDDPDARLTDDEIYANVLTLLLAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlL 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 260 NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKG--IMVLLSIYGLhhNPKVWPNPEVFDPFRF-APGS 336
Cdd:cd11083  277 EALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTVV-GDIALPAGtpVFLLTRAAGL--DAEHFPDPEEFDPERWlDGAR 353

                        330
                 ....*....|....*...
gi 194390028 337 AQHSH---AFLPFSGGSR 351
Cdd:cd11083  354 AAEPHdpsSLLPFGAGPR 371
PLN02936 PLN02936
epsilon-ring hydroxylase
 24-351 3.21e-32

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 125.67  E-value: 3.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  24 GYGLLLLNGQTWFQHRRMLTPAFHydilKPYVGLMADSV-----RVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAF 98
Cdd:PLN02936  96 GSGFAIAEGELWTARRRAVVPSLH----RRYLSVMVDRVfckcaERLVEKLEPVALSGEAVNMEAKFSQLTLDVIGLSVF 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  99 SHQ-GSIQVDrnsQSYIQAISDLNNLVFSRVRN--AFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGE 175
Cdd:PLN02936 172 NYNfDSLTTD---SPVIQAVYTALKEAETRSTDllPYWKVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGE 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 176 L---EKIKRKGHLDFLDILLLAKMEngsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG 252
Cdd:PLN02936 249 ViegEEYVNDSDPSVLRFLLASREE----VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQ 324

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 253 dGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:PLN02936 325 -GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERF 403

                        330       340
                 ....*....|....*....|....
gi 194390028 333 -----APGSAQHSHAFLPFSGGSR 351
Cdd:PLN02936 404 dldgpVPNETNTDFRYIPFSGGPR 427
PTZ00404 PTZ00404
cytochrome P450; Provisional
 7-351 7.22e-32

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 124.83  E-value: 7.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   7 RSDPKS----HGSYrflapwiGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVF 82
Cdd:PTZ00404  95 SDRPKIpsikHGTF-------YHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQVDVLIESMKKIESSGETFEPR 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  83 QHVSLMTLDTIMKCAFSHQGSIQVDRNS---QSYIQAISDL-NNLVFSRVRNAFHQNDTIYSLtsagrWThracqlahQH 158
Cdd:PTZ00404 168 YYLTKFTMSAMFKYIFNEDISFDEDIHNgklAELMGPMEQVfKDLGSGSLFDVIEITQPLYYQ-----YL--------EH 234

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 159 TDQVI-QLRKAQLQKEGE-LEKIKRKGHLDFLDILLlakMENGSILSDKDLR--AEVDTFMFEGHDTTASGISWILYALA 234
Cdd:PTZ00404 235 TDKNFkKIKKFIKEKYHEhLKTIDPEVPRDLLDLLI---KEYGTNTDDDILSilATILDFFLAGVDTSATSLEWMVLMLC 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 235 THPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPDGRSLPKGIMVLLSIYG 313
Cdd:PTZ00404 312 NYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDIIIGGGHFIPKDAQILINYYS 391

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 194390028 314 LHHNPKVWPNPEVFDPFRFAPGSAqhSHAFLPFSGGSR 351
Cdd:PTZ00404 392 LGRNEKYFENPEQFDPSRFLNPDS--NDAFMPFSIGPR 427
PLN02738 PLN02738
carotene beta-ring hydroxylase
 23-351 7.65e-32

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 125.80  E-value: 7.65e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  23 IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHqg 102
Cdd:PLN02738 210 MGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQASDRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNY-- 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 103 siqvDRNSQSYIQAISDLnnlVFSRVRNAFHQNDTIY---------SLTSAGRWTHRACQLAHQHTDQVIQLRK-----A 168
Cdd:PLN02738 288 ----DFDSLSNDTGIVEA---VYTVLREAEDRSVSPIpvweipiwkDISPRQRKVAEALKLINDTLDDLIAICKrmveeE 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 169 QLQKEGELEKIKRKGHLDFLdilllakMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIH 248
Cdd:PLN02738 361 ELQFHEEYMNERDPSILHFL-------LASGDDVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVD 433

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 249 SLLGDGASiTWNHLDQMPYTTMCIKEALRLYPPVPG-IGRELSTPV--TFPDGRslpkGIMVLLSIYGLHHNPKVWPNPE 325
Cdd:PLN02738 434 SVLGDRFP-TIEDMKKLKYTTRVINESLRLYPQPPVlIRRSLENDMlgGYPIKR----GEDIFISVWNLHRSPKHWDDAE 508

                        330       340       350
                 ....*....|....*....|....*....|.
gi 194390028 326 VFDPFRFA-----PGSAQHSHAFLPFSGGSR 351
Cdd:PLN02738 509 KFNPERWPldgpnPNETNQNFSYLPFGGGPR 539
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
 163-335 1.77e-31

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: 122.74  E-value: 1.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 163 IQLRKAQLQKEgelEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 242
Cdd:cd11075  191 IRARRKRRASG---EADKDYTDFLLLDLLDLKEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQEK 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 243 CREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW 321
Cdd:cd11075  268 LYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHfLLPHAVTEDTVL-GGYDIPAGAEVNFNVAAIGRDPKVW 346

                        170
                 ....*....|....
gi 194390028 322 PNPEVFDPFRFAPG 335
Cdd:cd11075  347 EDPEEFKPERFLAG 360
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
 38-351 5.72e-30

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: 118.45  E-value: 5.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  38 HRRMLTPAF-------HYDILKPYVGLMadsvrvmLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSH-QGSIQvDRN 109
Cdd:cd11058   61 LRRLLAHAFsekalreQEPIIQRYVDLL-------VSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGEsFGCLE-NGE 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 110 SQSYIQAIsdLNNLVFSRVRNAFHQNDTIYSLTsagRWTHRAcqLAHQHTDQVIQLRKAQLQKEGELEKikrkGHLDFLD 189
Cdd:cd11058  133 YHPWVALI--FDSIKALTIIQALRRYPWLLRLL---RLLIPK--SLRKKRKEHFQYTREKVDRRLAKGT----DRPDFMS 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 190 iLLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTT 269
Cdd:cd11058  202 -YILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQLPYLN 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 270 MCIKEALRLYPPVP-GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ-----HSHAF 343
Cdd:cd11058  281 AVIQEALRLYPPVPaGLPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFefdndKKEAF 360


                 ....*...
gi 194390028 344 LPFSGGSR 351
Cdd:cd11058  361 QPFSVGPR 368
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
 37-351 1.61e-29

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: 117.61  E-value: 1.61e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  37 QHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeelLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQA 116
Cdd:cd20638   81 HRKKVIMRAFSREALENYVPVIQEEVRSSVNQW---LQSGPCVLVYPEVKRLMFRIAMRILLGFEPQQTDREQEQQLVEA 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 117 ISDLnnlvfsrVRNAFHQN-DTIYSLTSAGRwthRACQLAHQHTDQVIqlrKAQLQKEGELEKIKrkghlDFLDILLLAK 195
Cdd:cd20638  158 FEEM-------IRNLFSLPiDVPFSGLYRGL---RARNLIHAKIEENI---RAKIQREDTEQQCK-----DALQLLIEHS 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 196 MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHS--LLG----DGASITWNHLDQMPYTT 269
Cdd:cd20638  220 RRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgLLStkpnENKELSMEVLEQLKYTG 299

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 270 MCIKEALRLYPPVPGIGR-ELSTPVTfpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH--AFLPF 346
Cdd:cd20638  300 CVIKETLRLSPPVPGGFRvALKTFEL--NGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSrfSFIPF 377


                 ....*
gi 194390028 347 SGGSR 351
Cdd:cd20638  378 GGGSR 382
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
 62-351 4.35e-28

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: 113.42  E-value: 4.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  62 VRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFS---HQGSIQVDRNSQSYIQAISDLNNLVfsrvrNAFHQNDTI 138
Cdd:cd20618   89 LSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGkryFGESEKESEEAREFKELIDEAFELA-----GAFNIGDYI 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 139 YSLtsagRW-----THRACQLAHQHTDQVIQlrkAQLQKEGELEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDT 213
Cdd:cd20618  164 PWL----RWldlqgYEKRMKKLHAKLDRFLQ---KIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLD 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 214 FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTP 292
Cdd:cd20618  237 MLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPlLLPHESTED 316

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194390028 293 VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSHaFLPFSGGSR 351
Cdd:cd20618  317 CKV-AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIddvkgQDFE-LLPFGSGRR 378
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
 146-351 8.30e-28

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: 112.63  E-value: 8.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 146 RWTHRACQLAHQHTDQVIQLRKAQLQKEGElekikRKGHLDFLDILLLAKMENGSiLSDKDLRAevdtFMFE----GHDT 221
Cdd:cd11073  177 RRMAEHFGKLFDIFDGFIDERLAEREAGGD-----KKKDDDLLLLLDLELDSESE-LTRNHIKA----LLLDlfvaGTDT 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 222 TASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPG-IGRELSTPVTFpDGRS 300
Cdd:cd11073  247 TSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLlLPRKAEEDVEV-MGYT 325

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 194390028 301 LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ---HSHAFLPFSGGSR 351
Cdd:cd11073  326 IPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDfkgRDFELIPFGSGRR 379
PLN02655 PLN02655
ent-kaurene oxidase
 165-351 1.48e-27

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 112.53  E-value: 1.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 165 LRKAQLQKEGELEKikRKGHLDFLdilllakMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 244
Cdd:PLN02655 230 LIKQQKKRIARGEE--RDCYLDFL-------LSEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLY 300

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 245 EEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNP 324
Cdd:PLN02655 301 REIREVCGDER-VTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENP 379

                        170       180
                 ....*....|....*....|....*....
gi 194390028 325 EVFDPFRFAPGSAQHS--HAFLPFSGGSR 351
Cdd:PLN02655 380 EEWDPERFLGEKYESAdmYKTMAFGAGKR 408
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
 62-351 1.61e-27

cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome P450 family 71 (CYP71) proteins, as well as some CYPs designated as belonging to a different family including CYP99A1, CYP83B1, and CYP84A1, among others. Characterized CYP71 enzymes include: parsnip (Pastinaca sativa) CYP71AJ4, also called angelicin synthase, that converts (+)-columbianetin to angelicin, an angular furanocumarin; periwinkle (Catharanthus roseus) CYP71D351, also called tabersonine 16-hydroxylase 2, that is involved in the foliar biosynthesis of vindoline; sorghum CYP71E1, also called 4-hydroxyphenylacetaldehyde oxime monooxygenase, that catalyzes the conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile; as well as maize CYP71C1, CYP71C2, and CYP71C4, which are monooxygenases catalyzing the oxidation of 3-hydroxyindolin-2-one, indolin-2-one, and indole, respectively. CYPs within a single CYP71 subfamily, such as the C subfamily, usually metabolize similar/related compounds. The CYP71-like family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410695 [Multi-domain]  Cd Length: 428  Bit Score: 111.79  E-value: 1.61e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  62 VRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFshqGSIQVDRNSQSYIQAISDLNNLV--F-------------- 125
Cdd:cd11072   91 VSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAF---GRKYEGKDQDKFKELVKEALELLggFsvgdyfpslgwidl 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 126 -----SRVRNAFHQNDTIYsltsagrwthracqlahqhtDQVIQLRKAQLQKEGElekikrKGHLDFLDILLLAKMENGS 200
Cdd:cd11072  168 ltgldRKLEKVFKELDAFL--------------------EKIIDEHLDKKRSKDE------DDDDDDLLDLRLQKEGDLE 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 201 I-LSDKDLRAEV-DtfMFE-GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALR 277
Cdd:cd11072  222 FpLTRDNIKAIIlD--MFLaGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLR 299

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194390028 278 LYPPVPGIG-RELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA---QHSHAFLPFSGGSR 351
Cdd:cd11072  300 LHPPAPLLLpRECREDCKI-NGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIdfkGQDFELIPFGAGRR 376
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
 153-351 5.86e-27

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: 110.04  E-value: 5.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 153 QLAHQHTDQVIQlrkaqlQKEGELEKIKRKGHLDFLDILLLAKMEngsiLSDKDLRAEVDTFMFEGHDTTASGISWILYA 232
Cdd:cd11062  181 ESIAKQVDEVLR------QVSAGDPPSIVTSLFHALLNSDLPPSE----KTLERLADEAQTLIGAGTETTARTLSVATFH 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 233 LATHPKHQERCREEIHSLLGDGASI-TWNHLDQMPYTTMCIKEALRLYPPVPG-----IGRElstPVTFpDGRSLPKGIM 306
Cdd:cd11062  251 LLSNPEILERLREELKTAMPDPDSPpSLAELEKLPYLTAVIKEGLRLSYGVPTrlprvVPDE---GLYY-KGWVIPPGTP 326

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194390028 307 VLLSIYGLHHNPKVWPNPEVFDPFR-FAPGSAQHSHAFL-PFSGGSR 351
Cdd:cd11062  327 VSMSSYFVHHDEEIFPDPHEFRPERwLGAAEKGKLDRYLvPFSKGSR 373
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
 186-351 4.23e-26

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: 107.65  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLaKMEN-----GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 260
Cdd:cd11026  202 DFIDCFLL-KMEKekdnpNSEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLE 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 261 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 337
Cdd:cd11026  281 DRAKMPYTDAVIHEVQRFGDIVPlGVPHAVTRDTKF-RGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFldEQGKF 359

                        170
                 ....*....|....
gi 194390028 338 QHSHAFLPFSGGSR 351
Cdd:cd11026  360 KKNEAFMPFSAGKR 373
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
 214-351 6.10e-26

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: 107.62  E-value: 6.10e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 214 FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPV 293
Cdd:cd20649  269 FLIAGYETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDC 348

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 294 TFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH--AFLPFSGGSR 351
Cdd:cd20649  349 VV-LGQRIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHpfVYLPFGAGPR 407
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
 181-351 2.02e-25

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: 105.97  E-value: 2.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 181 RKGHLDFLDILLLAKMEN--GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT 258
Cdd:cd20657  201 RKGKPDFLDFVLLENDDNgeGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLL 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 259 WNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGsa 337
Cdd:cd20657  281 ESDIPNLPYLQAICKETFRLHPSTPlNLPRIASEACEV-DGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPG-- 357

                        170       180
                 ....*....|....*....|....
gi 194390028 338 qhSHA----------FLPFSGGSR 351
Cdd:cd20657  358 --RNAkvdvrgndfeLIPFGAGRR 379
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
 203-350 3.10e-25

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: 105.41  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 203 SDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPP 281
Cdd:cd11082  217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDePPLTLDLLEEMKYTRQVVKEVLRYRPP 296

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194390028 282 VPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPkvWPNPEVFDPFRFAPGSA---QHSHAFLPFSGGS 350
Cdd:cd11082  297 APMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQedrKYKKNFLVFGAGP 366
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
 141-350 3.10e-25

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: 105.45  E-value: 3.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 141 LTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEgelekiKRKGHLDFLDILllakMENGSILSDKDLRAEVDTFM---FE 217
Cdd:cd11041  169 FLPEPRRLRRLLRRARPLIIPEIERRRKLKKGP------KEDKPNDLLQWL----IEAAKGEGERTPYDLADRQLalsFA 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 218 GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFP 296
Cdd:cd11041  239 AIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLvSLRRKVLKDVTLS 318

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194390028 297 DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-----PGSAQHSHA------FLPFSGGS 350
Cdd:cd11041  319 DGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYrlreqPGQEKKHQFvstspdFLGFGHGR 383
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
 186-351 5.07e-25

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: 104.61  E-value: 5.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDiLLLAKMENG----SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNH 261
Cdd:cd20651  202 DLID-AYLREMKKKeppsSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVVGRDRLPTLDD 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 262 LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQH 339
Cdd:cd20651  281 RSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFldEDGKLLK 360

                        170
                 ....*....|..
gi 194390028 340 SHAFLPFSGGSR 351
Cdd:cd20651  361 DEWFLPFGAGKR 372
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
 218-351 3.56e-24

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: 102.49  E-value: 3.56e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 218 GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFp 296
Cdd:cd20652  246 GVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPlGIPHGCTEDAVL- 324

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194390028 297 DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSR 351
Cdd:cd20652  325 AGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEAFIPFQTGKR 381
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
 31-351 4.74e-24

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: 101.99  E-value: 4.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  31 NGQTWFQHRRMLTPAFHYDILKPYVGLMADSV----RVMLDKWEELLGQDSPL----EVFQHVSlmtlDTIMKCAFSHQg 102
Cdd:cd11028   57 YGPRWKLHRKLAQNALRTFSNARTHNPLEEHVteeaEELVTELTENNGKPGPFdprnEIYLSVG----NVICAICFGKR- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 103 siqVDRNSQSYIQAISdlNNLVFSRVRNAFHQNDTIYSLTSAGRWTHRAcqlahqhTDQVIQ-LRKAQLQKEGELEKIKR 181
Cdd:cd11028  132 ---YSRDDPEFLELVK--SNDDFGAFVGAGNPVDVMPWLRYLTRRKLQK-------FKELLNrLNSFILKKVKEHLDTYD 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 182 KGHL-DFLDILLLAKMEN------GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG 254
Cdd:cd11028  200 KGHIrDITDALIKASEEKpeeekpEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQAELDRVIGRE 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 255 ASITWNHLDQMPYTTMCIKEALRLYPPVPgigrelstpVTFP---------DGRSLPKGIMVLLSIYGLHHNPKVWPNPE 325
Cdd:cd11028  280 RLPRLSDRPNLPYTEAFILETMRHSSFVP---------FTIPhattrdttlNGYFIPKGTVVFVNLWSVNHDEKLWPDPS 350

                        330       340       350
                 ....*....|....*....|....*....|
gi 194390028 326 VFDPFRFAPGSAQ----HSHAFLPFSGGSR 351
Cdd:cd11028  351 VFRPERFLDDNGLldktKVDKFLPFGAGRR 380
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
 185-337 1.02e-23

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: 101.25  E-value: 1.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 185 LDFLDILLlaKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQ 264
Cdd:cd11076  205 EDDVDVLL--SLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAK 282

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194390028 265 MPYTTMCIKEALRLYPPVPGI--GReLSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 337
Cdd:cd11076  283 LPYLQAVVKETLRLHPPGPLLswAR-LAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEG 356
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
 171-351 1.04e-23

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: 101.13  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 171 QKEGELEKIKRKGHLDFLDILL-LAKMENGSI-LSDKDLRA-EVDTFMfEGHDTTASGISWILYALATHPKHQERCREEI 247
Cdd:cd20655  191 EHEEKRKKRKEGGSKDLLDILLdAYEDENAEYkITRNHIKAfILDLFI-AGTDTSAATTEWAMAELINNPEVLEKAREEI 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 248 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVF 327
Cdd:cd20655  270 DSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKI-NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEF 348

                        170       180       190
                 ....*....|....*....|....*....|...
gi 194390028 328 DPFRFAPGSA---------QHSHaFLPFSGGSR 351
Cdd:cd20655  349 KPERFLASSRsgqeldvrgQHFK-LLPFGSGRR 380
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
 209-351 1.28e-23

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: 100.95  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 209 AEVDTFMfEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRE 288
Cdd:cd20674  230 AVVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPH 308

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194390028 289 LSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-PGSAqhSHAFLPFSGGSR 351
Cdd:cd20674  309 RTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLePGAA--NRALLPFGCGAR 370
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
 37-351 2.57e-23

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


Pssm-ID: 410729 [Multi-domain]  Cd Length: 431  Bit Score: 99.91  E-value: 2.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  37 QHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeelLGQDSPLEVFQHVSLMTLDTIMKCAFS-HQGSIQVDRNSQSYIQ 115
Cdd:cd20636   82 QRRKVLARVFSRAALESYLPRIQDVVRSEVRGW---CRGPGPVAVYTAAKSLTFRIAVRILLGlRLEEQQFTYLAKTFEQ 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 116 AISDLNNLV----FSRVRNAFHQNDTIysltsagrwthracqlaHQHTDQVIQlrkaqlqkegelEKIKRK---GHLDFL 188
Cdd:cd20636  159 LVENLFSLPldvpFSGLRKGIKARDIL-----------------HEYMEKAIE------------EKLQRQqaaEYCDAL 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 189 DILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSL-LGDG-----ASITWNHL 262
Cdd:cd20636  210 DYMIHSARENGKELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVSHgLIDQcqccpGALSLEKL 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 263 DQMPYTTMCIKEALRLYPPVPGIGRelSTPVTFP-DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPG---SAQ 338
Cdd:cd20636  290 SRLRYLDCVVKEVLRLLPPVSGGYR--TALQTFElDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEreeSKS 367

                        330
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd20636  368 GRFNYIPFGGGVR 380
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
 182-351 5.89e-23

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: 99.23  E-value: 5.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 182 KGHLDFLDILLLAKMENGSIL-SDKD--LRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT 258
Cdd:cd20654  214 KNDEDDDDVMMLSILEDSQISgYDADtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLKKAQEELDTHVGKDRWVE 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 259 WNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ 338
Cdd:cd20654  294 ESDIKNLVYLQAIVKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERFLTTHKD 373

                        170
                 ....*....|....*...
gi 194390028 339 -----HSHAFLPFSGGSR 351
Cdd:cd20654  374 idvrgQNFELIPFGSGRR 391
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
 161-351 6.36e-23

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: 98.93  E-value: 6.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKRKGHL--DFLDILLLAKM----------ENGSILSDKDLRAEVDTFMFEGHDTTASGISW 228
Cdd:cd20673  175 QCVKIRDKLLQKKLEEHKEKFSSDSirDLLDALLQAKMnaennnagpdQDSVGLSDDHILMTVGDIFGAGVETTTTVLKW 254

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 229 ILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPgigreLSTP-VTFPD----GRSLPK 303
Cdd:cd20673  255 IIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAP-----LLIPhVALQDssigEFTIPK 329

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 194390028 304 GIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH----SHAFLPFSGGSR 351
Cdd:cd20673  330 GTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQlispSLSYLPFGAGPR 381
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
 151-351 8.09e-23

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


Pssm-ID: 410751 [Multi-domain]  Cd Length: 444  Bit Score: 98.59  E-value: 8.09e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 151 ACQLAHQHTDQVIQLRkAQLQKEGELEKIKrkghlDFLDILLLAKMENGS-ILSDKDLRAEVDTFMFEGHDTTASGISWI 229
Cdd:cd20658  187 AMRIIRKYHDPIIDER-IKQWREGKKKEEE-----DWLDVFITLKDENGNpLLTPDEIKAQIKELMIAAIDNPSNAVEWA 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 230 LYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLL 309
Cdd:cd20658  261 LAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLL 340

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194390028 310 SIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSHAFLPFSGGSR 351
Cdd:cd20658  341 SRYGLGRNPKVWDDPLKFKPERHLNEDSevtltEPDLRFISFSTGRR 387
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
 186-351 1.25e-22

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: 97.92  E-value: 1.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLL-----AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 260
Cdd:cd20666  203 DFIDMYLLhieeeQKNNAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRAPSLT 282

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 261 HLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ-- 338
Cdd:cd20666  283 DKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFLDENGQli 362

                        170
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd20666  363 KKEAFIPFGIGRR 375
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
 24-347 2.03e-22

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: 97.18  E-value: 2.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  24 GYGLLLLNGQTWFQHRRmltpAFHYDILKP---------YVGLMADsvrvMLDKWEELLGQDSPLE-VFQHVSLMTLDTI 93
Cdd:cd20645   55 AYGLLILEGQEWQRVRS----AFQKKLMKPkevmkldgkINEVLAD----FMGRIDELCDETGRVEdLYSELNKWSFETI 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  94 MKCAFSHQ-GSIQ--VDRNSQSYIQAI----SDLNNLVFSRVRnaFHQNdtiyslTSAGRWthracqlaHQHT---DQVI 163
Cdd:cd20645  127 CLVLYDKRfGLLQqnVEEEALNFIKAIktmmSTFGKMMVTPVE--LHKR------LNTKVW--------QDHTeawDNIF 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 164 QLRKAQLQKEgeLEKIKRKGHLDFL-DILllakmeNGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 242
Cdd:cd20645  191 KTAKHCIDKR--LQRYSQGPANDFLcDIY------HDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQK 262

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 243 CREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWP 322
Cdd:cd20645  263 LLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKGTVLMINSQALGSSEEYFE 341

                        330       340
                 ....*....|....*....|....*
gi 194390028 323 NPEVFDPFRFapgsAQHSHAFLPFS 347
Cdd:cd20645  342 DGRQFKPERW----LQEKHSINPFA 362
PLN02302 PLN02302
ent-kaurenoic acid oxidase
 39-351 2.32e-22

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 97.86  E-value: 2.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  39 RRMLTPAFH-YDILKPYVGLMADSVRVMLDKWEELlgqdSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYiqai 117
Cdd:PLN02302 142 RRLTAAPVNgPEALSTYIPYIEENVKSCLEKWSKM----GEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREY---- 213

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 118 SDLNNLVFSRVRNAfhqndtiysltsAGRWTHRACQlAHQHTDQVIQL----RKAQlQKEGELEKIKrkghlDFLDILLL 193
Cdd:PLN02302 214 TTLNYGVRAMAINL------------PGFAYHRALK-ARKKLVALFQSivdeRRNS-RKQNISPRKK-----DMLDLLLD 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 194 AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE----IHSLLGDGASITWNHLDQMPYTT 269
Cdd:PLN02302 275 AEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEqeeiAKKRPPGQKGLTLKDVRKMEYLS 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 270 MCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQhSHAFLPFSGG 349
Cdd:PLN02302 355 QVIDETLRLINISLTVFREAKTDVEV-NGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPK-AGTFLPFGLG 432


                 ..
gi 194390028 350 SR 351
Cdd:PLN02302 433 SR 434
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
 180-349 2.53e-22

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 97.31  E-value: 2.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 180 KRKGHLDFLDiLLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGD---GAS 256
Cdd:PLN02196 239 RRQNGSSHND-LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeeGES 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 257 ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApgS 336
Cdd:PLN02196 318 LTWEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEY-EGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFE--V 394

                        170
                 ....*....|...
gi 194390028 337 AQHSHAFLPFSGG 349
Cdd:PLN02196 395 APKPNTFMPFGNG 407
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
 7-351 3.04e-22

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: 96.75  E-value: 3.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   7 RSDPKSHGSYRFLAPwIGYGLLLLNGQTWFQHRRMLTPAfhydILKP-----YVGLMADSVRVMLDKWEELLGQDSPLEV 81
Cdd:cd20648   40 RSDLSSWKDYRQLRG-HAYGLLTAEGEEWQRLRSLLAKH----MLKPkaveaYAGVLNAVVTDLIRRLRRQRSRSSPGVV 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  82 -----------FQHVSLMTLDTIMKCAfshqgSIQVDRNSQSYIQAIsdlnNLVFsrvrnafhqndTIYSLTSA-GRWTH 149
Cdd:cd20648  115 kdiagefykfgLEGISSVLFESRIGCL-----EANVPEETETFIQSI----NTMF-----------VMTLLTMAmPKWLH 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 150 RA--------CQ-------LAHQHTDQVIQLRKAQLQkEGELEKIKrkgHLDFLdillLAKMEngsiLSDKDLRAEVDTF 214
Cdd:cd20648  175 RLfpkpwqrfCRswdqmfaFAKGHIDRRMAEVAAKLP-RGEAIEGK---YLTYF----LAREK----LPMKSIYGNVTEL 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 215 MFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVT 294
Cdd:cd20648  243 LLAGVDTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDI 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194390028 295 FPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHSHAFLPFSGGSR 351
Cdd:cd20648  323 QVGEYIIPKKTLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHPYASLPFGFGKR 380
PLN02687 PLN02687
flavonoid 3'-monooxygenase
 162-351 4.83e-22

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 96.80  E-value: 4.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 162 VIQLRKAQLQKEGElekikrkGHLDFLDiLLLAKMEN------GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALAT 235
Cdd:PLN02687 255 IIEEHKAAGQTGSE-------EHKDLLS-TLLALKREqqadgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIR 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 236 HPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPpvpgigrelSTPVTFP---------DGRSLPKGIM 306
Cdd:PLN02687 327 HPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHP---------STPLSLPrmaaeeceiNGYHIPKGAT 397

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 194390028 307 VLLSIYGLHHNPKVWPNPEVFDPFRFAPGSaqhSHA----------FLPFSGGSR 351
Cdd:PLN02687 398 LLVNVWAIARDPEQWPDPLEFRPDRFLPGG---EHAgvdvkgsdfeLIPFGAGRR 449
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
 11-351 1.63e-21

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: 94.78  E-value: 1.63e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  11 KSHGSY--RF-LAPWIGY--------GLLLLNGQTWFQHRRML-TPAFHYDILKPYVGLMADSVR---VMLDKWEELLGQ 75
Cdd:cd20643   31 KSEGMFpeRLsVPPWVAYrdyrkrkyGVLLKNGEAWRKDRLILnKEVLAPKVIDNFVPLLNEVSQdfvSRLHKRIKKSGS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  76 DS-PLEVFQHVSLMTLDTIMKCAFSH-QGSIQ--VDRNSQSYIQAISdlnnLVFSRVRNAFHQNDTIYSLTSAGRWTHR- 150
Cdd:cd20643  111 GKwTADLSNDLFRFALESICNVLYGErLGLLQdyVNPEAQRFIDAIT----LMFHTTSPMLYIPPDLLRLINTKIWRDHv 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 151 -ACQLAHQHTDQVIQLRKAQLQKegelekiKRKGHLDFLDIL--LLAKmengSILSDKDLRAEVDTFMFEGHDTTASGIS 227
Cdd:cd20643  187 eAWDVIFNHADKCIQNIYRDLRQ-------KGKNEHEYPGILanLLLQ----DKLPIEDIKASVTELMAGGVDTTSMTLQ 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 228 WILYALATHPKHQERCREEI----HSLLGDGASItwnhLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPK 303
Cdd:cd20643  256 WTLYELARNPNVQEMLRAEVlaarQEAQGDMVKM----LKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYH-IPA 330

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 194390028 304 GIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAfLPFSGGSR 351
Cdd:cd20643  331 GTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN-LGFGFGPR 377
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
 169-351 2.13e-21

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 94.89  E-value: 2.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 169 QLQKEGELEKIKRKGHLDFLDILLLAKMENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 247
Cdd:PLN03112 258 DEHRRARSGKLPGGKDMDFVDVLLSLPGENGKEhMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEEL 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 248 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV 326
Cdd:PLN03112 338 DSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPfLIPHESLRATTI-NGYYIPAKTRVFINTHGLGRNTKIWDDVEE 416

                        170       180       190
                 ....*....|....*....|....*....|..
gi 194390028 327 FDPFRFAPG-----SAQHSHAF--LPFSGGSR 351
Cdd:PLN03112 417 FRPERHWPAegsrvEISHGPDFkiLPFSAGKR 448
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
 7-351 5.13e-21

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: 93.19  E-value: 5.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028   7 RSDPKSHGSYRFLAPWiGYGLLLLNGQTWFQHRRMLTPAfhydILKP-----YVGLMADSVRVMLDKWEELlGQDSPLEV 81
Cdd:cd20646   39 RSDMPHWKEHRDLRGH-AYGPFTEEGEKWYRLRSVLNQR----MLKPkevslYADAINEVVSDLMKRIEYL-RERSGSGV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  82 FqhVSLMTlDTIMKCAFSHQGSI-----------QVDRNSQSYIQAIsdlnnlvfsrvRNAFHQNDTIYSLTsagRWTHR 150
Cdd:cd20646  113 M--VSDLA-NELYKFAFEGISSIlfetrigclekEIPEETQKFIDSI-----------GEMFKLSEIVTLLP---KWTRP 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 151 ACQLAHQHTD----------QVIQLRKAQLQKEGELEKIKRKGHLDFLdilllakMENGSiLSDKDLRAEVDTFMFEGHD 220
Cdd:cd20646  176 YLPFWKRYVDawdtifsfgkKLIDKKMEEIEERVDRGEPVEGEYLTYL-------LSSGK-LSPKEVYGSLTELLLAGVD 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 221 TTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRS 300
Cdd:cd20646  248 TTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVGDYL 327

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194390028 301 LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSR 351
Cdd:cd20646  328 FPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrDGGLKHHPFGSIPFGYGVR 380
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
 88-332 8.62e-21

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 93.31  E-value: 8.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  88 MTLDTIMKCAFSHQ-GSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAgRWTHRACQLAHQHTDQVIQLR 166
Cdd:PLN03195 177 MTLDSICKVGFGVEiGTLSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSE-ALLSKSIKVVDDFTYSVIRRR 255

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 167 KAQLQK-EGELEKIKRkghlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCRE 245
Cdd:PLN03195 256 KAEMDEaRKSGKKVKH----DILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYS 331

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 246 EIHSLLGDGAS--------------------ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGI 305
Cdd:PLN03195 332 ELKALEKERAKeedpedsqsfnqrvtqfaglLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGG 411

                        250       260
                 ....*....|....*....|....*...
gi 194390028 306 MVLLSIYGLHHNPKVW-PNPEVFDPFRF 332
Cdd:PLN03195 412 MVTYVPYSMGRMEYNWgPDAASFKPERW 439
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
 186-351 1.59e-20

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: 91.78  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILL--LAK-MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHL 262
Cdd:cd20662  202 DFIDAYLkeMAKyPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADR 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 263 DQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHS 340
Cdd:cd20662  282 ESMPYTNAVIHEVQRMGNIIPlNVPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFlENGQFKKR 360

                        170
                 ....*....|.
gi 194390028 341 HAFLPFSGGSR 351
Cdd:cd20662  361 EAFLPFSMGKR 371
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
 165-351 1.63e-20

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: 91.83  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 165 LRKAQLQKegeLEKIKRKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 244
Cdd:cd20637  188 LEKAIREK---LQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLR 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 245 EEI--HSLLGDG----ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRelSTPVTFP-DGRSLPKGIMVLLSIYGLHHN 317
Cdd:cd20637  265 EELrsNGILHNGclceGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYR--TALQTFElDGFQIPKGWSVLYSIRDTHDT 342

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 194390028 318 PKVWPNPEVFDPFRFAPGSAQHSHA---FLPFSGGSR 351
Cdd:cd20637  343 APVFKDVDAFDPDRFGQERSEDKDGrfhYLPFGGGVR 379
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
 191-350 2.25e-20

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


Pssm-ID: 410707 [Multi-domain]  Cd Length: 406  Bit Score: 91.35  E-value: 2.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 191 LLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLlgDGASITWNHLDQMPYTTM 270
Cdd:cd20614  193 LIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEA 270

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 271 CIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFapgsAQHSHAFLP----- 345
Cdd:cd20614  271 LFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERW----LGRDRAPNPvellq 345


                 ....*
gi 194390028 346 FSGGS 350
Cdd:cd20614  346 FGGGP 350
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
 157-351 2.89e-20

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: 91.01  E-value: 2.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 157 QHTDQVIQLRKAQLQKEgELEKIKRKGHLDFLDILLLAKMENGsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATH 236
Cdd:cd20656  184 KHGARRDRLTKAIMEEH-TLARQKSGGGQQHFVALLTLKEQYD--LSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRN 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 237 PKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHH 316
Cdd:cd20656  261 PRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIAR 340

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 194390028 317 NPKVWPNPEVFDPFRFAPGSAQ---HSHAFLPFSGGSR 351
Cdd:cd20656  341 DPAVWKNPLEFRPERFLEEDVDikgHDFRLLPFGAGRR 378
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
 187-351 4.19e-20

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: 90.64  E-value: 4.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 187 FLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMP 266
Cdd:cd20661  219 YLDEMDQNKNDPESTFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPSFEDKCKMP 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 267 YTTMCIKEALRLYPPVP-GIGRELSTPvTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAF 343
Cdd:cd20661  299 YTEAVLHEVLRFCNIVPlGIFHATSKD-AVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFLDSNGQfaKKEAF 377


                 ....*...
gi 194390028 344 LPFSGGSR 351
Cdd:cd20661  378 VPFSLGRR 385
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
 200-351 5.01e-20

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: 90.45  E-value: 5.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 200 SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKH--QERCREEIHSLLGDGASITWNHLDQM--PYTTMCIKEA 275
Cdd:cd11066  222 SKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGQeiQEKAYEEILEAYGNDEDAWEDCAAEEkcPYVVALVKET 301

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 194390028 276 LRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSR 351
Cdd:cd11066  302 LRYFTVLPlGLPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWldASGDLIPGPPHFSFGAGSR 379
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
 26-351 2.66e-19

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: 88.36  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  26 GLLLLNGQTWFQHRRmltpaFHYDILKPY-VGLMADSVRVMLDKWE--ELLGQDSPLEVFQHVSLM--TLDTIMKCAFSH 100
Cdd:cd20667   51 GIICTNGLTWKQQRR-----FCMTTLRELgLGKQALESQIQHEAAElvKVFAQENGRPFDPQDPIVhaTANVIGAVVFGH 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 101 QGSIQvDRNSQSYIQAIsdlnNLVFSRVRNAFHQndtiysLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIK 180
Cdd:cd20667  126 RFSSE-DPIFLELIRAI----NLGLAFASTIWGR------LYDAFPWLMRYLPGPHQKIFAYHDAVRSFIKKEVIRHELR 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 181 RKGH-LDFLDILLL----AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGA 255
Cdd:cd20667  195 TNEApQDFIDCYLAqitkTKDDPVSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQ 274

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 256 SITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-- 332
Cdd:cd20667  275 LICYEDRKRLPYTNAVIHEVQRLSNVVSvGAVRQCVTSTTM-HGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFld 353

                        330
                 ....*....|....*....
gi 194390028 333 APGSAQHSHAFLPFSGGSR 351
Cdd:cd20667  354 KDGNFVMNEAFLPFSAGHR 372
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
 220-351 6.88e-19

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 87.48  E-value: 6.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 220 DTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR 299
Cdd:PLN02394 307 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGY 386

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194390028 300 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAqHSHA------FLPFSGGSR 351
Cdd:PLN02394 387 DIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA-KVEAngndfrFLPFGVGRR 443
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
 180-351 5.76e-18

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 84.90  E-value: 5.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 180 KRKGHLDFLDILLlAKMEN--GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASI 257
Cdd:PLN00110 262 ERKGNPDFLDVVM-ANQENstGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 258 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 337
Cdd:PLN00110 341 VESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKN 420

                        170       180
                 ....*....|....*....|
gi 194390028 338 Q------HSHAFLPFSGGSR 351
Cdd:PLN00110 421 AkidprgNDFELIPFGAGRR 440
PLN02183 PLN02183
ferulate 5-hydroxylase
 160-351 1.64e-17

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 83.36  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 160 DQVIQLRKAQLQKEGELEkikrkGHLDFLDILLLAKMENGSILSDKDLRAEVD-----------TFMFEGHDTTASGISW 228
Cdd:PLN02183 252 DDHIQKRKNQNADNDSEE-----AETDMVDDLLAFYSEEAKVNESDDLQNSIKltrdnikaiimDVMFGGTETVASAIEW 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 229 ILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPvTFPDGRSLPKGIMVL 308
Cdd:PLN02183 327 AMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAED-AEVAGYFIPKRSRVM 405

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 194390028 309 LSIYGLHHNPKVWPNPEVFDPFRF----APGSAQHSHAFLPFSGGSR 351
Cdd:PLN02183 406 INAWAIGRDKNSWEDPDTFKPSRFlkpgVPDFKGSHFEFIPFGSGRR 452
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
 228-349 8.21e-17

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: 80.87  E-value: 8.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 228 WILYALATHPKHQERCREEIHSLLGDGASITWNH-----LDQMPYTTMCIKEALRLYPpVPGIGRELSTPVTFPDGRSLP 302
Cdd:cd11040  245 WLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltdlLTSCPLLDSTYLETLRLHS-SSTSVRLVTEDTVLGGGYLLR 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194390028 303 KGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF-----APGSAQHSHAFLPFSGG 349
Cdd:cd11040  324 KGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkdgDKKGRGLPGAFRPFGGG 376
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
 215-351 9.37e-17

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


Pssm-ID: 410746 [Multi-domain]  Cd Length: 420  Bit Score: 80.73  E-value: 9.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 215 MFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVT 294
Cdd:cd20653  236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDC 315

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194390028 295 FPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFLPFSGGSR 351
Cdd:cd20653  316 KIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFE-GEEREGYKLIPFGLGRR 371
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
 158-332 2.20e-16

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: 79.58  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 158 HTDQVIQLRKAQLQKEGELekikrKGHLdfLDILLLAKMengsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATHP 237
Cdd:cd20647  201 HVDNRLREIQKQMDRGEEV-----KGGL--LTYLLVSKE-----LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHP 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 238 KHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRelstpVTFPD----GRSLPKGIMVLLSIYG 313
Cdd:cd20647  269 EVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGR-----VTQDDlivgGYLIPKGTQLALCHYS 343

                        170
                 ....*....|....*....
gi 194390028 314 LHHNPKVWPNPEVFDPFRF 332
Cdd:cd20647  344 TSYDEENFPRAEEFRPERW 362
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
 176-351 2.34e-16

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: 79.61  E-value: 2.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 176 LEKIKRkgHLDFLDI--------LLLAKM--ENGSILSD---KDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 242
Cdd:cd20665  185 LEKVKE--HQESLDVnnprdfidCFLIKMeqEKHNQQSEftlENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAK 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 243 CREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW 321
Cdd:cd20665  263 VQEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPnNLPHAVTCDTKF-RNYLIPKGTTVITSLTSVLHDDKEF 341

                        170       180       190
                 ....*....|....*....|....*....|..
gi 194390028 322 PNPEVFDPFRF--APGSAQHSHAFLPFSGGSR 351
Cdd:cd20665  342 PNPEKFDPGHFldENGNFKKSDYFMPFSAGKR 373
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
 220-351 2.43e-16

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: 79.44  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 220 DTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR 299
Cdd:cd11074  247 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGY 326

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194390028 300 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSHAFLPFSGGSR 351
Cdd:cd11074  327 DIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESkveanGNDFRYLPFGVGRR 383
PLN02971 PLN02971
tryptophan N-hydroxylase
 157-351 3.83e-16

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 79.31  E-value: 3.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 157 QHTDQVIQLRkAQLQKEGELEKIKrkghlDFLDILLLAKMENGS-ILSDKDLRAEVDTFMFEGHDTTASGISWILYALAT 235
Cdd:PLN02971 283 KYHDPIIDER-IKMWREGKRTQIE-----DFLDIFISIKDEAGQpLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMIN 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 236 HPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLH 315
Cdd:PLN02971 357 KPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLG 436

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 194390028 316 HNPKVWPNPEVFDPFRFAPGSA-----QHSHAFLPFSGGSR 351
Cdd:PLN02971 437 RNPKVWSDPLSFKPERHLNECSevtltENDLRFISFSTGKR 477
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
 186-332 6.37e-16

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


Pssm-ID: 410768 [Multi-domain]  Cd Length: 434  Bit Score: 78.51  E-value: 6.37e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLA-----KMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG--ASIT 258
Cdd:cd20675  210 DMMDAFILAlekgkSGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDrlPCIE 289

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194390028 259 wnhlDQ--MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20675  290 ----DQpnLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRF 361
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
 228-349 1.20e-15

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: 77.35  E-value: 1.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 228 WILYALATHPKHQERCREEIHSLLGDG----ASITWNHLDQMPYTTMCIKEALRLYPPvpG-IGRELSTPVTFPDgRSLP 302
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKAgkdkIKISEDDLKKMPYIKRCVLEAIRLRSP--GaITRKVVKPIKIKN-YTIP 308

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 194390028 303 KGIMVLLSIYGLHHNPKVWPNPEVFDPFR----------FAPGsaqhshaFLPFSGG 349
Cdd:cd20635  309 AGDMLMLSPYWAHRNPKYFPDPELFKPERwkkadleknvFLEG-------FVAFGGG 358
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
 186-351 1.30e-15

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: 77.54  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMEN----GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGdGASITWNH 261
Cdd:cd20664  201 GFIDAFLVKQQEEeessDSFFHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQVEH 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 262 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQ 338
Cdd:cd20664  280 RKNMPYTDAVIHEIQRFANIVPmNLPHATTRDVTF-RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFldSQGKFV 358

                        170
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd20664  359 KRDAFMPFSAGRR 371
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
 186-351 1.35e-15

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: 77.49  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLlAKM--ENGSILS---DKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 260
Cdd:cd20669  202 DFIDCFL-TKMaeEKQDPLShfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLE 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 261 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 337
Cdd:cd20669  281 DRARMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNF-RGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFldDNGSF 359

                        170
                 ....*....|....
gi 194390028 338 QHSHAFLPFSGGSR 351
Cdd:cd20669  360 KKNDAFMPFSAGKR 373
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
 199-331 1.78e-15

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 77.42  E-value: 1.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 199 GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALR 277
Cdd:PLN02426 286 ASINDDKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEVASAIREEADRVMGPNqEAASFEEMKEMHYLHAALYESMR 365

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 194390028 278 LYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFR 331
Cdd:PLN02426 366 LFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRMERIWgPDCLEFKPER 420
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
 186-350 4.17e-15

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: 75.72  E-value: 4.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEiHSLLGDGasitwnhldqm 265
Cdd:cd11078  189 DLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD-PSLIPNA----------- 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 266 pyttmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfaPGSAQHshafLP 345
Cdd:cd11078  257 ------VEETLRYDSPVQGLRRTATRDVEI-GGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--PNARKH----LT 323


                 ....*
gi 194390028 346 FSGGS 350
Cdd:cd11078  324 FGHGI 328
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
 163-351 6.69e-15

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: 75.22  E-value: 6.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 163 IQLRKAQLQKEGELEKI------KRKGHLD------FLDILLLAKMENG---SILSDKDLRAEVDTFMFEGHDTTASGIS 227
Cdd:cd20671  165 LKLHKPILDKVEEVCMIlrtlieARRPTIDgnplhsYIEALIQKQEEDDpkeTLFHDANVLACTLDLVMAGTETTSTTLQ 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 228 WILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMV 307
Cdd:cd20671  245 WAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKGTPV 323

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 194390028 308 LLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSR 351
Cdd:cd20671  324 IPLLSSVLLDKTQWETPYQFNPNHFldAEGKFVKKEAFLPFSAGRR 369
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
 25-351 7.35e-15

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 75.40  E-value: 7.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  25 YGLLLLNGQTwfqHRRM--LTPAF-HYDILKPYVGLMADS-VRVMLDKWEellgqdSPLEVFQHVSLMTLDTIMKCAFSH 100
Cdd:PLN02987 115 HSLLLMKGNL---HKKMhsLTMSFaNSSIIKDHLLLDIDRlIRFNLDSWS------SRVLLMEEAKKITFELTVKQLMSF 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 101 QGSIQVDRNSQSYIQAISDLNNLVFSrvrnafhqndtIYSLTsagrwTHRACQlAHQHTDQVIQLRKAQLQKEGELEKIK 180
Cdd:PLN02987 186 DPGEWTESLRKEYVLVIEGFFSVPLP-----------LFSTT-----YRRAIQ-ARTKVAEALTLVVMKRRKEEEEGAEK 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 181 RKghlDFLDILLLAkmenGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE---IHSLLGDGASI 257
Cdd:PLN02987 249 KK---DMLAALLAS----DDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEhekIRAMKSDSYSL 321

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 258 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA--PG 335
Cdd:PLN02987 322 EWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEV-KGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQsnSG 400

                        330
                 ....*....|....*.
gi 194390028 336 SAQHSHAFLPFSGGSR 351
Cdd:PLN02987 401 TTVPSNVFTPFGGGPR 416
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
 192-351 1.77e-14

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: 74.11  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 192 LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMC 271
Cdd:cd20644  218 IVAELLLQAELSLEAIKANITELTAGGVDTTAFPLLFTLFELARNPDVQQILRQESLAAAAQISEHPQKALTELPLLKAA 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 272 IKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP--GSAQHSHAfLPFSGG 349
Cdd:cd20644  298 LKETLRLYPVGITVQRVPSSDLVLQNYH-IPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDirGSGRNFKH-LAFGFG 375


                 ..
gi 194390028 350 SR 351
Cdd:cd20644  376 MR 377
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
 214-349 1.79e-14

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: 73.65  E-value: 1.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 214 FMFEghdttASGISWI--LYALATHPKHQERCREEIHSLLGDGAsitwnhldqMPYTTMCIKEALRLYPPVPGIGRELST 291
Cdd:cd20624  202 FAFD-----AAGMALLraLALLAAHPEQAARAREEAAVPPGPLA---------RPYLRACVLDAVRLWPTTPAVLRESTE 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 194390028 292 PvTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGG 349
Cdd:cd20624  268 D-TVWGGRTVPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPDEGLVPFSAG 324
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
 226-349 2.11e-14

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: 73.72  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 226 ISWILYALATHPKHQERCREeihsllgdgasitwnhlDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGI 305
Cdd:cd11067  240 VTFAALALHEHPEWRERLRS-----------------GDEDYAEAFVQEVRRFYPFFPFVGARARRDFEW-QGYRFPKGQ 301

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 194390028 306 MVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFLPFSGG 349
Cdd:cd11067  302 RVLLDLYGTNHDPRLWEDPDRFRPERFL-GWEGDPFDFIPQGGG 344
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
 200-332 2.24e-14

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: 73.59  E-value: 2.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 200 SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLY 279
Cdd:cd20677  230 AVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHS 309

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 194390028 280 PPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20677  310 SFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERF 362
PLN02774 PLN02774
brassinosteroid-6-oxidase
 163-351 7.35e-14

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 72.12  E-value: 7.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 163 IQLRKAQLQKEGELEKIKRKGHLDFLDIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 240
Cdd:PLN02774 219 VQARKNIVRMLRQLIQERRASGETHTDMLgyLMRKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKAL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 241 ERCREEiHSLLGDGAS----ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHH 316
Cdd:PLN02774 299 QELRKE-HLAIRERKRpedpIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMEL-NGYVIPKGWRIYVYTREINY 376

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194390028 317 NPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSR 351
Cdd:PLN02774 377 DPFLYPDPMTFNPWRWLDKSLESHNYFFLFGGGTR 411
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
 186-349 8.17e-14

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: 71.56  E-value: 8.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMEnGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEiHSLLGdgasitwnhldqm 265
Cdd:cd20629  173 DLISRLLRAEVE-GEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRD-RSLIP------------- 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 266 pyttMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsAQHSHafLP 345
Cdd:cd20629  238 ----AAIEEGLRWEPPVASVPRMALRDVEL-DGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-----KPKPH--LV 305


                 ....
gi 194390028 346 FSGG 349
Cdd:cd20629  306 FGGG 309
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
 186-351 1.48e-13

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: 71.37  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMEN----GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNH 261
Cdd:cd20668  202 DFIDSFLIRMQEEkknpNTEFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFED 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 262 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA--PGSAQ 338
Cdd:cd20668  282 RAKMPYTEAVIHEIQRFGDVIPmGLARRVTKDTKF-RDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLddKGQFK 360

                        170
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd20668  361 KSDAFVPFSIGKR 373
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
 164-348 3.71e-13

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: 69.85  E-value: 3.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 164 QLRKAQLQKEGELEKI--KRKG----HLDFLDILLLAKMENGSILSDKDLraevdtFMFEGHDTTASGISWILYALATHP 237
Cdd:cd20627  160 QYEDALMEMESVLKKVikERKGknfsQHVFIDSLLQGNLSEQQVLEDSMI------FSLAGCVITANLCTWAIYFLTTSE 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 238 KHQERCREEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRL--YPPVPGIGRELSTPVtfpDGRSLPKGIMVLLSIYGLH 315
Cdd:cd20627  234 EVQKKLYKEVDQVLGKGP-ITLEKIEQLRYCQQVLCETVRTakLTPVSARLQELEGKV---DQHIIPKETLVLYALGVVL 309

                        170       180       190
                 ....*....|....*....|....*....|...
gi 194390028 316 HNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSG 348
Cdd:cd20627  310 QDNTTWPLPYRFDPDRFDDESVMKSFSLLGFSG 342
PLN00168 PLN00168
Cytochrome P450; Provisional
 166-335 6.38e-13

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 69.59  E-value: 6.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 166 RKAQLQKEGELEKIKRKGHLDFLDILLLAKM--ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERC 243
Cdd:PLN00168 264 YKNHLGQGGEPPKKETTFEHSYVDTLLDIRLpeDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKL 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 244 REEIHSLLGDGA-SITWNHLDQMPYTTMCIKEALRLYPP----VPGIGRElstpvtfpD----GRSLPKGIMVLLSIYGL 314
Cdd:PLN00168 344 HDEIKAKTGDDQeEVSEEDVHKMPYLKAVVLEGLRKHPPahfvLPHKAAE--------DmevgGYLIPKGATVNFMVAEM 415

                        170       180
                 ....*....|....*....|.
gi 194390028 315 HHNPKVWPNPEVFDPFRFAPG 335
Cdd:PLN00168 416 GRDEREWERPMEFVPERFLAG 436
PLN03018 PLN03018
homomethionine N-hydroxylase
 152-351 6.96e-13

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 69.27  E-value: 6.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 152 CQLAHQHTDQVIQLRKAQLQKEGELEKIKrkghlDFLDILLLAKMENGSILSDKD-LRAEVDTFMFEGHDTTASGISWIL 230
Cdd:PLN03018 264 VNLVRSYNNPIIDERVELWREKGGKAAVE-----DWLDTFITLKDQNGKYLVTPDeIKAQCVEFCIAAIDNPANNMEWTL 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 231 YALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLS 310
Cdd:PLN03018 339 GEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVC 418

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 194390028 311 IYGLHHNPKVWPNPEVFDPFRFAPGSA--------QHSHAFLPFSGGSR 351
Cdd:PLN03018 419 RPGLGRNPKIWKDPLVYEPERHLQGDGitkevtlvETEMRFVSFSTGRR 467
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
 189-349 9.86e-13

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: 68.35  E-value: 9.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 189 DIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREeihsllgdgasitwnHLDQMP 266
Cdd:cd20625  182 DLIsaLVAAEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLRA---------------DPELIP 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 267 YTtmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSaqhshafLPF 346
Cdd:cd20625  247 AA---VEELLRYDSPVQLTARVALEDVEI-GGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRAPNRH-------LAF 315


                 ...
gi 194390028 347 SGG 349
Cdd:cd20625  316 GAG 318
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
 186-351 1.43e-12

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: 68.03  E-value: 1.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLaKM--ENGSILSDKDLRAEVDT---FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 260
Cdd:cd20670  202 DFIDCFLI-KMhqDKNNPHTEFNLKNLVLTtlnLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVD 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 261 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 337
Cdd:cd20670  281 DRVKMPYTDAVIHEIQRLTDIVPlGVPHNVIRDTQF-RGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQGRF 359

                        170
                 ....*....|....
gi 194390028 338 QHSHAFLPFSGGSR 351
Cdd:cd20670  360 KKNEAFVPFSSGKR 373
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
 186-351 2.74e-12

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: 67.41  E-value: 2.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLlAKMENG-----SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 260
Cdd:cd20663  206 DLTDAFL-AEMEKAkgnpeSSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMA 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 261 HLDQMPYTTMCIKEALRLYPPVPgigreLSTP-VTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--A 333
Cdd:cd20663  285 DQARMPYTNAVIHEVQRFGDIVP-----LGVPhMTSRDievqGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFldA 359

                        170
                 ....*....|....*...
gi 194390028 334 PGSAQHSHAFLPFSGGSR 351
Cdd:cd20663  360 QGHFVKPEAFMPFSAGRR 377
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
 31-351 3.08e-12

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: 67.00  E-value: 3.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  31 NGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSplevfqHVSLMTLdtiMKCafshqgsIQVDRNS 110
Cdd:cd20616   66 NPALWKKVRPFFAKALTGPGLVRMVTVCVESTNTHLDNLEEVTNESG------YVDVLTL---MRR-------IMLDTSN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 111 QSYIQAISDLNNLVFsRVRNAFH-------QNDTIYSLtsagRWTHRACQLAHQHTDQVI-----QLRKAQLQKEgelek 178
Cdd:cd20616  130 RLFLGVPLNEKAIVL-KIQGYFDawqalliKPDIFFKI----SWLYKKYEKAVKDLKDAIeilieQKRRRISTAE----- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 179 iKRKGHLDFLDILLLAkmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDgASIT 258
Cdd:cd20616  200 -KLEDHMDFATELIFA--QKRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE-RDIQ 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 259 WNHLDQMPYTTMCIKEALRLYPPVPGIGRE-LSTPVTfpDGRSLPKGIMVLLSIyGLHHNPKVWPNPEVFDPFRFA---P 334
Cdd:cd20616  276 NDDLQKLKVLENFINESMRYQPVVDFVMRKaLEDDVI--DGYPVKKGTNIILNI-GRMHRLEFFPKPNEFTLENFEknvP 352

                        330
                 ....*....|....*..
gi 194390028 335 gsaqhSHAFLPFSGGSR 351
Cdd:cd20616  353 -----SRYFQPFGFGPR 364
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
 31-331 5.96e-12

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: 66.55  E-value: 5.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  31 NGQTWFQHRRML----TPAFHYDILKPYvglMADSVRVMLDKWEE--LLGQDSPLEVFQHVSLMTLDTIMKCAFshqGSI 104
Cdd:cd20622   58 TGPAFRKHRSLVqdlmTPSFLHNVAAPA---IHSKFLDLIDLWEAkaRLAKGRPFSAKEDIHHAALDAIWAFAF---GIN 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 105 QVDRNSQSYIQAISDLNNLV---------------FSRVRNAFHQ-NDTI-YSLTSagrWTHRacqLAHQHTDQVIQLRK 167
Cdd:cd20622  132 FDASQTRPQLELLEAEDSTIlpagldepvefpeapLPDELEAVLDlADSVeKSIKS---PFPK---LSHWFYRNQPSYRR 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 168 AQLQKE----GELEKIKRKGHLDFLDI-------------LLLAKMENGSILSDKD-LRAEVDTFMFEGHDTTASGISWI 229
Cdd:cd20622  206 AAKIKDdflqREIQAIARSLERKGDEGevrsavdhmvrreLAAAEKEGRKPDYYSQvIHDELFGYLIAGHDTTSTALSWG 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 230 LYALATHPKHQERCREEIHSLL----GDGASITWNHLDQM--PYTTMCIKEALRLYPPVPGIGRELSTPVTFPdGRSLPK 303
Cdd:cd20622  286 LKYLTANQDVQSKLRKALYSAHpeavAEGRLPTAQEIAQAriPYLDAVIEEILRCANTAPILSREATVDTQVL-GYSIPK 364

                        330       340
                 ....*....|....*....|....*....
gi 194390028 304 GIMVLLSIYGlhhnPKVW-PNPEVFDPFR 331
Cdd:cd20622  365 GTNVFLLNNG----PSYLsPPIEIDESRR 389
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
 24-351 6.67e-12

cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is composed of cytochrome P450 monooxygenases that are part of gene clusters involved in the biosynthesis of various compounds such as mycotoxins and alkaloids, including Aspergillus fumigatus gliotoxin biosynthesis protein (GliC), Penicillium rubens roquefortine/meleagrin synthesis protein R (RoqR), Aspergillus oryzae aspirochlorine biosynthesis protein C (AclC), Aspergillus terreus bimodular acetylaranotin synthesis protein ataTC, Kluyveromyces lactis pulcherrimin biosynthesis cluster protein 2 (PUL2), and Aspergillus nidulans aspyridones biosynthesis protein B (ApdB). The GliC-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410708 [Multi-domain]  Cd Length: 409  Bit Score: 66.16  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  24 GYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRvmldKWEELLGQDSP------LEVFQHVSLMTLDTIMKCA 97
Cdd:cd20615   49 GQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFSREAR----KWVQNLPTNSGdgrrfvIDPAQALKFLPFRVIAEIL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028  98 FshqGSIqvdrnSQSYIQAISDLNNL-------VFSRVRNAFhqndTIYSL--TSAGRwthracQLAHQHTDQVIQLRKA 168
Cdd:cd20615  125 Y---GEL-----SPEEKEELWDLAPLreelfkyVIKGGLYRF----KISRYlpTAANR------RLREFQTRWRAFNLKI 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 169 QlqkegeleKIKRKGHLDFLDILLLAKMENGSIlSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIH 248
Cdd:cd20615  187 Y--------NRARQRGQSTPIVKLYEAVEKGDI-TFEELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEIS 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 249 SLLGDGASITWNHL-DQMPYTTMCIKEALRLYPpvpgigrelSTPVTFP---------DGRSLPKGIMVLLSIYGLHHN- 317
Cdd:cd20615  258 AAREQSGYPMEDYIlSTDTLLAYCVLESLRLRP---------LLAFSVPessptdkiiGGYRIPANTPVVVDTYALNINn 328

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 194390028 318 PKVWPNPEVFDPFRFA-PGSAQHSHAFLPFSGGSR 351
Cdd:cd20615  329 PFWGPDGEAYRPERFLgISPTDLRYNFWRFGFGPR 363
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
 186-351 1.45e-11

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: 65.18  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLL----AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNH 261
Cdd:cd20672  202 DFIDTYLLrmekEKSNHHTEFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDD 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 262 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQ 338
Cdd:cd20672  282 RAKMPYTDAVIHEIQRFSDLIPiGVPHRVTKDTLF-RGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFldANGALK 360

                        170
                 ....*....|...
gi 194390028 339 HSHAFLPFSGGSR 351
Cdd:cd20672  361 KSEAFMPFSTGKR 373
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
 146-331 1.74e-11

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: 64.51  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 146 RWTHRACQLAHqHTDQVIQLRKAQLQKE-GELEKIKRKGHLDflDIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTT 222
Cdd:cd11031  146 AWSDALLSTSA-LTPEEAEAARQELRGYmAELVAARRAEPGD--DLLsaLVAARDDDDRLSEEELVTLAVGLLVAGHETT 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 223 ASGISWILYALATHPKHQERCREEiHSLLGDGasitwnhldqmpyttmcIKEALRLYPPVPGIG--RELSTPVTFPDGRs 300
Cdd:cd11031  223 ASQIGNGVLLLLRHPEQLARLRAD-PELVPAA-----------------VEELLRYIPLGAGGGfpRYATEDVELGGVT- 283

                        170       180       190
                 ....*....|....*....|....*....|.
gi 194390028 301 LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11031  284 IRAGEAVLVSLNAANRDPEVFPDPDRLDLDR 314
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
 187-351 2.28e-11

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 64.71  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 187 FLDILL-LAKMENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQ 264
Cdd:PLN03234 267 FIDLLMqIYKDQPFSIkFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPN 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 265 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFA---PGSAQHS 340
Cdd:PLN03234 347 LPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMkehKGVDFKG 426

                        170
                 ....*....|...
gi 194390028 341 HAF--LPFSGGSR 351
Cdd:PLN03234 427 QDFelLPFGSGRR 439
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
 218-328 2.33e-11

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: 64.14  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 218 GHDTTASGISWILYALATHPKHQERCREEiHSLLgdgasitwnhldqmpytTMCIKEALRLYPPVPGIGRELSTPVTFpD 297
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPDQWERLRAD-PSLA-----------------PNAFEEAVRLESPVQTFSRTTTRDTEL-A 274

                         90       100       110
                 ....*....|....*....|....*....|.
gi 194390028 298 GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFD 328
Cdd:cd11037  275 GVTIPAGSRVLVFLGSANRDPRKWDDPDRFD 305
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
 186-331 2.63e-11

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: 64.09  E-value: 2.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLlgDGAsitwnhldqm 265
Cdd:cd11029  192 DLLSALVAAR-DEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRADPELW--PAA---------- 258

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 194390028 266 pyttmcIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11029  259 ------VEELLRYDGPVAlATLRFATEDVEV-GGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR 318
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
 203-351 3.11e-11

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 64.26  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 203 SDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDgasitwNHLDQMPYTTMCIKEALRLYPPV 282
Cdd:PLN02169 298 KDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN------EDLEKLVYLHAALSESMRLYPPL 371

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194390028 283 PGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV-FDPFRFAP--GSAQH--SHAFLPFSGGSR 351
Cdd:PLN02169 372 PFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISdnGGLRHepSYKFMAFNSGPR 445
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
 186-331 4.99e-11

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: 63.39  E-value: 4.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMENGSiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGdgasitwnhldqm 265
Cdd:cd11032  179 DLISRLVEAEVDGER-LTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLIPG------------- 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194390028 266 pyttmCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11032  245 -----AIEEVLRYRPPVQRTARVTTEDVEL-GGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR 304
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
 164-349 1.10e-10

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: 62.10  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 164 QLRKAQLQKEGELEKIKRK----GHlDFLDILLLAKMeNGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKH 239
Cdd:cd11080  149 GLRCAEQLSQYLLPVIEERrvnpGS-DLISILCTAEY-EGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQ 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 240 QERCREEiHSLLgdgasitwnhldqmpytTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPK 319
Cdd:cd11080  227 LAAVRAD-RSLV-----------------PRAIAETLRYHPPVQLIPRQASQDVVVSGME-IKKGTTVFCLIGAANRDPA 287

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 194390028 320 VWPNPEVFDPFR--------FAPgSAQHshafLPFSGG 349
Cdd:cd11080  288 AFEDPDTFNIHRedlgirsaFSG-AADH----LAFGSG 320
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
 197-337 1.23e-10

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: 62.34  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 197 ENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEA 275
Cdd:cd20676  227 ENANIqLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILET 306

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194390028 276 LRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 337
Cdd:cd20676  307 FRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFltADGTE 370
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
 186-333 1.31e-10

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


Pssm-ID: 410660 [Multi-domain]  Cd Length: 361  Bit Score: 61.97  E-value: 1.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMeNGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPkhQERCReeihsLLGDGASItwnhldqm 265
Cdd:cd11034  171 DLISRLIEGEI-DGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHP--EDRRR-----LIADPSLI-------- 234

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 194390028 266 pytTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA 333
Cdd:cd11034  235 ---PNAVEEFLRFYSPVAGLARTVTQEVEV-GGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTP 298
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
 186-331 1.39e-10

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: 62.06  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEiHSLLGDGasitwnhldqm 265
Cdd:cd20630  184 DLLTTLLRAE-EDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE-PELLRNA----------- 250

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 266 pyttmcIKEALRLyppvPGIGRELSTPVTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd20630  251 ------LEEVLRW----DNFGKMGTARYATEDvelcGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR 310
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
 186-331 1.80e-10

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


Pssm-ID: 410661 [Multi-domain]  Cd Length: 359  Bit Score: 61.45  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 186 DFLDILLLAKMEnGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREeihsllgDGASItwnhldqm 265
Cdd:cd11035  171 DLISAILNAEID-GRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRE-------DPELI-------- 234

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 194390028 266 pytTMCIKEALRLYPPVpGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11035  235 ---PAAVEELLRRYPLV-NVARIVTRDVEF-HGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR 295
PLN02966 PLN02966
cytochrome P450 83A1
 206-351 3.35e-10

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 61.30  E-value: 3.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 206 DLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAS--ITWNHLDQMPYTTMCIKEALRLYPPVP 283
Cdd:PLN02966 289 NVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGStfVTEDDVKNLPYFRALVKETLRIEPVIP 368

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194390028 284 GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQHS---HAFLPFSGGSR 351
Cdd:PLN02966 369 LLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKgtdYEFIPFGSGRR 440
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
 229-332 3.68e-10

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: 60.74  E-value: 3.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 229 ILYALATHPKH-QERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP---GIGRELSTpVTFPDGR-SLPK 303
Cdd:cd11071  248 LLARLGLAGEElHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPlqyGRARKDFV-IESHDASyKIKK 326

                         90       100
                 ....*....|....*....|....*....
gi 194390028 304 GIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd11071  327 GELLVGYQPLATRDPKVFDNPDEFVPDRF 355
PLN02500 PLN02500
cytochrome P450 90B1
 165-351 2.16e-09

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 58.72  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 165 LRKAQLQKEGELEKIKrKGHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 244
Cdd:PLN02500 239 LKFIERKMEERIEKLK-EEDESVEEDDLLGWVLKHSNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELR 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 245 EE------IHSLLGDgASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNP 318
Cdd:PLN02500 318 EEhleiarAKKQSGE-SELNWEDYKKMEFTQCVINETLRLGNVVRFLHRKALKDVRY-KGYDIPSGWKVLPVIAAVHLDS 395

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 194390028 319 KVWPNPEVFDPFRF-----APGSAQHSHA----FLPFSGGSR 351
Cdd:PLN02500 396 SLYDQPQLFNPWRWqqnnnRGGSSGSSSAttnnFMPFGGGPR 437
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
 272-350 3.53e-09

cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a putative cytochrome P450 of unknown function. Cytochrome P450 (P450, CYP) is a large superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop. Their monooxygenase activity relies on the reductive scission of molecular oxygen bound to the P450 heme iron, and the delivery of two electrons to the heme iron during the catalytic cycle.


Pssm-ID: 410719  Cd Length: 381  Bit Score: 57.80  E-value: 3.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 272 IKEALRLYPPVPGIGRelstpvTFPDgRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGS 350
Cdd:cd20626  262 VKEALRLYPPTRRIYR------AFQR-PGSSKPEIIAADIEACHRSESIWgPDALEFNPSRWSKLTPTQKEAFLPFGSGP 334
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
 161-351 4.67e-09

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 57.44  E-value: 4.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 161 QVIQLRKAQLQKEGELEKIKRKghlDFLDILLlakMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 240
Cdd:PLN03141 212 KIIEEKRRAMKNKEEDETGIPK---DVVDVLL---RDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVAL 285

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 241 ERCREE---IHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHH 316
Cdd:PLN03141 286 QQLTEEnmkLKRLKADtGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEI-KGYLIPKGWCVLAYFRSVHL 364

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 194390028 317 NPKVWPNPEVFDPFRFAPGSAQHShAFLPFSGGSR 351
Cdd:PLN03141 365 DEENYDNPYQFNPWRWQEKDMNNS-SFTPFGGGQR 398
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
 150-328 4.98e-09

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


Pssm-ID: 410664 [Multi-domain]  Cd Length: 382  Bit Score: 56.99  E-value: 4.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 150 RACQLAHQHTDQVIQLRKAQLQKegelekikrkghlDFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWI 229
Cdd:cd11038  172 AAVEELYDYADALIEARRAEPGD-------------DLISTLVAAE-QDGDRLSDEELRNLIVALLFAGVDTTRNQLGLA 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 230 LYALATHPKHQERCREeiHSLLGDGAsitwnhldqmpyttmcIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLL 309
Cdd:cd11038  238 MLTFAEHPDQWRALRE--DPELAPAA----------------VEEVLRWCPTTTWATREAVEDVEYNGVT-IPAGTVVHL 298

                        170
                 ....*....|....*....
gi 194390028 310 SIYGLHHNPKVWPnPEVFD 328
Cdd:cd11038  299 CSHAANRDPRVFD-ADRFD 316
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
 189-331 5.06e-08

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


Pssm-ID: 410659 [Multi-domain]  Cd Length: 378  Bit Score: 54.07  E-value: 5.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 189 DIL-LLAKME-NGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPkhqercrEEIHSLLGDGAsitwnHLDQMp 266
Cdd:cd11033  190 DLIsVLANAEvDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHP-------DQWERLRADPS-----LLPTA- 256

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194390028 267 yttmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11033  257 -----VEEILRWASPVIHFRRTATRDTEL-GGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR 315
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
 274-331 6.25e-08

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: 53.88  E-value: 6.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 194390028 274 EALRLYPPVPGIGRELSTPVTFPDG----RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd20612  246 EALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR 307
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
 191-331 6.49e-08

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 53.51  E-value: 6.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 191 LLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEihsllgdgasitwnhLDQMPyttM 270
Cdd:cd11079  168 RLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLRAN---------------PALLP---A 229

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 194390028 271 CIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11079  230 AIDEILRLDDPFVANRRITTRDVEL-GGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR 289
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
 228-332 6.57e-06

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: 6.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 228 WILYALATHPKHQERCREEIHSLLGDGA---------SITWNHLDQMPYTTMCIKEALRL--YPPVPGIGRELSTpVTFP 296
Cdd:cd20632  237 WAMYYLLRHPEALAAVRDEIDHVLQSTGqelgpdfdiHLTREQLDSLVYLESAINESLRLssASMNIRVVQEDFT-LKLE 315

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 194390028 297 DGRS--LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20632  316 SDGSvnLRKGDIVALYPQSLHMDPEIYEDPEVFKFDRF 353
PLN02648 PLN02648
allene oxide synthase
 226-332 3.82e-05

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 45.31  E-value: 3.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 226 ISWIlyALAThPKHQERCREEIHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPgigrelstpvtFPDGRslPKG 304
Cdd:PLN02648 296 LKWV--GRAG-EELQARLAEEVRSAVKAgGGGVTFAALEKMPLVKSVVYEALRIEPPVP-----------FQYGR--ARE 359

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 194390028 305 IMVLLS------------IYGLH----HNPKVWPNPEVFDPFRF 332
Cdd:PLN02648 360 DFVIEShdaafeikkgemLFGYQplvtRDPKVFDRPEEFVPDRF 403
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
 189-328 1.10e-03

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: 40.58  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 189 DIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHslLGDGAsitwnhldqmp 266
Cdd:cd11030  189 DLLsrLVAEHGAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRADPS--LVPGA----------- 255

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 194390028 267 yttmcIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFD 328
Cdd:cd11030  256 -----VEELLRYLSIVQdGLPRVATEDVEI-GGVTIRAGEGVIVSLPAANRDPAVFPDPDRLD 312
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
 127-332 1.45e-03

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: 40.44  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 127 RVRNA---FHQNDTIYSLTSAGRWTHrACQLAHQHTDQVIQ-LRKAQLQK-EGELEKIKRKGHLDfldilllakmENGSI 201
Cdd:cd20631  154 LILNAlenFKEFDKVFPALVAGLPIH-MFKTAKSAREALAErLLHENLQKrENISELISLRMLLN----------DTLST 222

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 202 LSDKDL-RAEVDTfMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG--------DGASITWN--HLDQMPYTTM 270
Cdd:cd20631  223 LDEMEKaRTHVAM-LWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEktgqkvsdGGNPIVLTreQLDDMPVLGS 301

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 194390028 271 CIKEALRLYPPVPGIGRELS-TPVTFPDGRSLP--KGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20631  302 IIKEALRLSSASLNIRVAKEdFTLHLDSGESYAirKDDIIALYPQLLHLDPEIYEDPLTFKYDRY 366
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
 259-331 1.62e-03

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: 39.78  E-value: 1.62e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 194390028 259 WNHLDQMPYT-TMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 331
Cdd:cd11036  211 WARLRPDPELaAAAVAETLRYDPPVRLERRFAAEDLEL-AGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGR 283
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
 175-332 7.69e-03

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


Pssm-ID: 410726 [Multi-domain]  Cd Length: 449  Bit Score: 38.12  E-value: 7.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 175 ELEKIKRKghldFLDILLLAKM---ENGS-ILSDKD-LRAEV-------DTFMF----EGHDTTASGISWILYALATHPK 238
Cdd:cd20633  181 EAERLKRL----FWDMLSVSKMsqkENISgWISEQQrQLAEHgmpeymqDRFMFlllwASQGNTGPASFWLLLYLLKHPE 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194390028 239 HQERCREEIHSLL----------GDGASITWNHLDQMPYTTMCIKEALRLyPPVPGIGRELSTPVTF--PDGR--SLPKG 304
Cdd:cd20633  257 AMKAVREEVEQVLketgqevkpgGPLINLTRDMLLKTPVLDSAVEETLRL-TAAPVLIRAVVQDMTLkmANGReyALRKG 335

                        170       180
                 ....*....|....*....|....*....
gi 194390028 305 IMVLLSIY-GLHHNPKVWPNPEVFDPFRF 332
Cdd:cd20633  336 DRLALFPYlAVQMDPEIHPEPHTFKYDRF 364
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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