NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|158937242|ref|NP_000769|]
View 

cytochrome P450 4A11 isoform 1 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
74-505 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: 935.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYD 153
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 154 ILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVR 233
Cdd:cd20678   83 ILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 234 NAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRA 313
Cdd:cd20678  163 NFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 314 EVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGREL 393
Cdd:cd20678  243 EVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISREL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 394 STPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSRNCIGKQFAMNELKVAT 471
Cdd:cd20678  323 SKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPRNCIGQQFAMNEMKVAV 402
                        410       420       430
                 ....*....|....*....|....*....|....
gi 158937242 472 ALTLLRFELLPDPTRIPIPIARLVLKSKNGIHLR 505
Cdd:cd20678  403 ALTLLRFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
74-505 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: 935.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYD 153
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 154 ILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVR 233
Cdd:cd20678   83 ILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 234 NAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRA 313
Cdd:cd20678  163 NFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 314 EVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGREL 393
Cdd:cd20678  243 EVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISREL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 394 STPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSRNCIGKQFAMNELKVAT 471
Cdd:cd20678  323 SKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPRNCIGQQFAMNEMKVAV 402
                        410       420       430
                 ....*....|....*....|....*....|....
gi 158937242 472 ALTLLRFELLPDPTRIPIPIARLVLKSKNGIHLR 505
Cdd:cd20678  403 ALTLLRFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
52-505 1.53e-150

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: 438.64  E-value: 1.53e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242   52 PCPPSHWLFGHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSD------PKSHGSYRFLAP 125
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGeefsgrPDEPWFATSRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  126 WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ 205
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  206 GSIQVDRNSQSYIQAISDLNNLV-FSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGelekik 284
Cdd:pfam00067 162 FGSLEDPKFLELVKAVQELSSLLsSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAK------ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  285 rKRHLDFLDILLLAKM-ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITW 363
Cdd:pfam00067 236 -KSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  364 NHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPdGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP--GS 440
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDenGK 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158937242  441 AQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPI---ARLVLKSKNGIHLR 505
Cdd:pfam00067 394 FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIdetPGLLLPPKPYKLKF 461
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
88-508 3.71e-60

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: 203.59  E-value: 3.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  88 HWLWGGKVR-VQLYDPDYMKVILGRSD--PKSHGSYRFLAP--WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLM 162
Cdd:COG2124   35 FRVRLPGGGaWLVTRYEDVREVLRDPRtfSSDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 163 ADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQGSiqvDRNSqsyiqaisdlnnlvFSRVRNAFHQNDTI 242
Cdd:COG2124  115 REIADELLDRLAA----RGPVDLVEEFARPLPVIVICELLGVPEE---DRDR--------------LRRWSDALLDALGP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 243 YSLTSAGRwTHRACQLAHQHTDQVIQLRKAQLQKegelekikrkrhlDFLDILLLAKmENGSILSDKDLRAEVDTFMFEG 322
Cdd:COG2124  174 LPPERRRR-ARRARAELDAYLRELIAERRAEPGD-------------DLLSALLAAR-DDGERLSDEELRDELLLLLLAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 323 HDTTASGISWILYALATHPKHQERCREEIhsllgdgasitwnhldqmPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDG 402
Cdd:COG2124  239 HETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GG 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 403 RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsaqHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELL- 481
Cdd:COG2124  300 VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPDLr 372
                        410       420
                 ....*....|....*....|....*..
gi 158937242 482 PDPTRIPIPIARLVLKSKNGIHLRLRR 508
Cdd:COG2124  373 LAPPEELRWRPSLTLRGPKSLPVRLRP 399
PLN02290 PLN02290
cytokinin trans-hydroxylase
110-509 1.00e-45

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 167.68  E-value: 1.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 110 GRSDPKSHGSYRFlapwIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQ-DSPLEVFQH 188
Cdd:PLN02290 127 GKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESgQTEVEIGEY 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 189 VSLMTLDTIMKCAFSHQgsiqVDRNSQSYiQAISDLNNLVFSRVRNAF---------HQNDTIYSLTSagrwthracqla 259
Cdd:PLN02290 203 MTRLTADIISRTEFDSS----YEKGKQIF-HLLTVLQRLCAQATRHLCfpgsrffpsKYNREIKSLKG------------ 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 260 hqhtdQVIQLRKAQLQKEGELEKIKRKR-HLDFLDILLLAKME----NGSILSDKDLRAEVDTFMFEGHDTTASGISWIL 334
Cdd:PLN02290 266 -----EVERLLMEIIQSRRDCVEIGRSSsYGDDLLGMLLNEMEkkrsNGFNLNLQLIMDECKTFFFAGHETTALLLTWTL 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 335 YALATHPKHQERCREEIHSLLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLS 414
Cdd:PLN02290 341 MLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIP 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 415 IYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIAR 493
Cdd:PLN02290 419 VLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNYRHAPVVV 498
                        410
                 ....*....|....*.
gi 158937242 494 LVLKSKNGIHLRLRRL 509
Cdd:PLN02290 499 LTIKPKYGVQVCLKPL 514
 
Name Accession Description Interval E-value
CYP4B-like cd20678
cytochrome P450 family 4, subfamily B and similar cytochrome P450s, including subfamilies A, T, ...
74-505 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: 935.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYD 153
Cdd:cd20678    3 KILKWVEKYPYAFPLWFGGFKAFLNIYDPDYAKVVLSRSDPKAQGVYKFLIPWIGKGLLVLNGQKWFQHRRLLTPAFHYD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 154 ILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVR 233
Cdd:cd20678   83 ILKPYVKLMADSVRVMLDKWEKLATQDSSLEIFQHVSLMTLDTIMKCAFSHQGSCQLDGRSNSYIQAVSDLSNLIFQRLR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 234 NAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRA 313
Cdd:cd20678  163 NFFYHNDFIYKLSPHGRRFRRACQLAHQHTDKVIQQRKEQLQDEGELEKIKKKRHLDFLDILLFAKDENGKSLSDEDLRA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 314 EVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGREL 393
Cdd:cd20678  243 EVDTFMFEGHDTTASGISWILYCLALHPEHQQRCREEIREILGDGDSITWEHLDQMPYTTMCIKEALRLYPPVPGISREL 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 394 STPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA--QHSHAFLPFSGGSRNCIGKQFAMNELKVAT 471
Cdd:cd20678  323 SKPVTFPDGRSLPAGITVSLSIYGLHHNPAVWPNPEVFDPLRFSPENSskRHSHAFLPFSAGPRNCIGQQFAMNEMKVAV 402
                        410       420       430
                 ....*....|....*....|....*....|....
gi 158937242 472 ALTLLRFELLPDPTRIPIPIARLVLKSKNGIHLR 505
Cdd:cd20678  403 ALTLLRFELLPDPTRIPIPIPQLVLKSKNGIHLY 436
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
83-505 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: 631.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  83 PSACPHWLWGGKVRVQLYDPDYMKVILGRSDPKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLM 162
Cdd:cd20659    1 PRAYVFWLGPFRPILVLNHPDTIKAVLKTSEPKDRDSYRFLKPWLGDGLLLSNGKKWKRNRRLLTPAFHFDILKPYVPVY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 163 ADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTI 242
Cdd:cd20659   81 NECTDILLEKWSKLAETGESVEVFEDISLLTLDIILRCAFSYKSNCQQTGKNHPYVAAVHELSRLVMERFLNPLLHFDWI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 243 YSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGElEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEG 322
Cdd:cd20659  161 YYLTPEGRRFKKACDYVHKFAEEIIKKRRKELEDNKD-EALSKRKYLDFLDILLTARDEDGKGLTDEEIRDEVDTFLFAG 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 323 HDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDG 402
Cdd:cd20659  240 HDTTASGISWTLYSLAKHPEHQQKCREEVDEVLGDRDDIEWDDLSKLPYLTMCIKESLRLYPPVPFIARTLTKPITI-DG 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 403 RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL 480
Cdd:cd20659  319 VTLPAGTLIAINIYALHHNPTVWEDPEEFDPERFLPENIKkrDPFAFIPFSAGPRNCIGQNFAMNEMKVVLARILRRFEL 398
                        410       420
                 ....*....|....*....|....*
gi 158937242 481 LPDPTRIPIPIARLVLKSKNGIHLR 505
Cdd:cd20659  399 SVDPNHPVEPKPGLVLRSKNGIKLK 423
CYP4F cd20679
cytochrome P450 family 4, subfamily F; Cytochrome P450 family 4, subfamily F (CYP4F) enzymes ...
74-505 0e+00

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


Pssm-ID: 410772 [Multi-domain]  Cd Length: 442  Bit Score: 532.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  74 RIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSD---PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAF 150
Cdd:cd20679    3 VVTQLVATYPQGCLWWLGPFYPIIRLFHPDYIRPVLLASAavaPKDELFYGFLKPWLGDGLLLSSGDKWSRHRRLLTPAF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 151 HYDILKPYVGLMADSVRVMLDKWEELLGQDSP-LEVFQHVSLMTLDTIMKCAFSHQGSIQvDRNSQsYIQAISDLNNLVF 229
Cdd:cd20679   83 HFNILKPYVKIFNQSTNIMHAKWRRLASEGSArLDMFEHISLMTLDSLQKCVFSFDSNCQ-EKPSE-YIAAILELSALVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 230 SRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRH---LDFLDILLLAKMENGSIL 306
Cdd:cd20679  161 KRQQQLLLHLDFLYYLTADGRRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLKAKAKsktLDFIDVLLLSKDEDGKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 307 SDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAS--ITWNHLDQMPYTTMCIKEALRLYP 384
Cdd:cd20679  241 SDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVQELLKDREPeeIEWDDLAQLPFLTMCIKESLRLHP 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 385 PVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH--SHAFLPFSGGSRNCIGKQF 462
Cdd:cd20679  321 PVTAISRCCTQDIVLPDGRVIPKGIICLISIYGTHHNPTVWPDPEVYDPFRFDPENSQGrsPLAFIPFSAGPRNCIGQTF 400
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 158937242 463 AMNELKVATALTLLRFELLPDpTRIPIPIARLVLKSKNGIHLR 505
Cdd:cd20679  401 AMAEMKVVLALTLLRFRVLPD-DKEPRRKPELILRAEGGLWLR 442
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
90-504 1.09e-165

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: 475.86  E-value: 1.09e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  90 LW-GGKVRVQLYDPDYMKVILGRSD--PKSHGsYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20628    6 LWiGPKPYVVVTNPEDIEVILSSSKliTKSFL-YDFLKPWLGDGLLTSTGEKWRKRRKLLTPAFHFKILESFVEVFNENS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 167 RVMLDKWEELLGQDSpLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSqSYIQAISDLNNLVFSRVRNAFHQNDTIYSLT 246
Cdd:cd20628   85 KILVEKLKKKAGGGE-FDIFPYISLCTLDIICETAMGVKLNAQSNEDS-EYVKAVKRILEIILKRIFSPWLRFDFIFRLT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 247 SAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEK----IKRKRHLDFLDILLLAKMENGSiLSDKDLRAEVDTFMFEG 322
Cdd:cd20628  163 SLGKEQRKALKVLHDFTNKVIKERREELKAEKRNSEeddeFGKKKRKAFLDLLLEAHEDGGP-LTDEDIREEVDTFMFAG 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 323 HDTTASGISWILYALATHPKHQERCREEIHSLLG-DGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpD 401
Cdd:cd20628  242 HDTTASAISFTLYLLGLHPEVQEKVYEELDEIFGdDDRRPTLEDLNKMKYLERVIKETLRLYPSVPFIGRRLTEDIKL-D 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 402 GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd20628  321 GYTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRFLPENSAkrHPYAYIPFSAGPRNCIGQKFAMLEMKTLLAKILRNFR 400
                        410       420
                 ....*....|....*....|....*.
gi 158937242 480 LLPDPTRIPI-PIARLVLKSKNGIHL 504
Cdd:cd20628  401 VLPVPPGEDLkLIAEIVLRSKNGIRV 426
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
52-505 1.53e-150

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: 438.64  E-value: 1.53e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242   52 PCPPSHWLFGHIQELQQDQELQRIQKWVETFPSACPHWLWGGKVRVQLYDPDYMKVILGRSD------PKSHGSYRFLAP 125
Cdd:pfam00067   2 PGPPPLPLFGNLLQLGRKGNLHSVFTKLQKKYGPIFRLYLGPKPVVVLSGPEAVKEVLIKKGeefsgrPDEPWFATSRGP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  126 WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ 205
Cdd:pfam00067  82 FLGKGIVFANGPRWRQLRRFLTPTFTSFGKLSFEPRVEEEARDLVEKLRKTAGEPGVIDITDLLFRAALNVICSILFGER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  206 GSIQVDRNSQSYIQAISDLNNLV-FSRVRNAFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGelekik 284
Cdd:pfam00067 162 FGSLEDPKFLELVKAVQELSSLLsSPSPQLLDLFPILKYFPGPHGRKLKRARKKIKDLLDKLIEERRETLDSAK------ 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  285 rKRHLDFLDILLLAKM-ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITW 363
Cdd:pfam00067 236 -KSPRDFLDALLLAKEeEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEIDEVIGDKRSPTY 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  364 NHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPdGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP--GS 440
Cdd:pfam00067 315 DDLQNMPYLDAVIKETLRLHPVVPlLLPREVTKDTVIP-GYLIPKGTLVIVNLYALHRDPEVFPNPEEFDPERFLDenGK 393
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158937242  441 AQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPI---ARLVLKSKNGIHLR 505
Cdd:pfam00067 394 FRKSFAFLPFGAGPRNCLGERLARMEMKLFLATLLQNFEVELPPGTDPPDIdetPGLLLPPKPYKLKF 461
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
89-504 3.41e-133

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: 393.17  E-value: 3.41e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  89 WLwGGKVRVQLYDPDYMKVILGRSD--PKSHgSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20660    7 WL-GPKPIVVLYSAETVEVILSSSKhiDKSF-EYDFLHPWLGTGLLTSTGEKWHSRRKMLTPTFHFKILEDFLDVFNEQS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 167 RVMLDKWEELLGqDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQsYIQAISDLNNLVFSRVRNAFHQNDTIYSLT 246
Cdd:cd20660   85 EILVKKLKKEVG-KEEFDIFPYITLCALDIICETAMGKSVNAQQNSDSE-YVKAVYRMSELVQKRQKNPWLWPDFIYSLT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 247 SAGrWTHRAC-QLAHQHTDQVIQLRKAQLQKEGELEK-------IKRKRHLDFLDILLLAKmENGSILSDKDLRAEVDTF 318
Cdd:cd20660  163 PDG-REHKKClKILHGFTNKVIQERKAELQKSLEEEEeddedadIGKRKRLAFLDLLLEAS-EEGTKLSDEDIREEVDTF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 319 MFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPV 397
Cdd:cd20660  241 MFEGHDTTAAAINWALYLIGSHPEVQEKVHEELDRIFGDSdRPATMDDLKEMKYLECVIKEALRLFPSVPMFGRTLSEDI 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 398 TFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTL 475
Cdd:cd20660  321 EI-GGYTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFLPENSAgrHPYAYIPFSAGPRNCIGQKFALMEEKVVLSSIL 399
                        410       420       430
                 ....*....|....*....|....*....|
gi 158937242 476 LRFELLPDPTRIPI-PIARLVLKSKNGIHL 504
Cdd:cd20660  400 RNFRIESVQKREDLkPAGELILRPVDGIRV 429
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
101-504 1.46e-98

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: 303.35  E-value: 1.46e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 101 DPDYMKVIL---GRSDPKShGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELl 177
Cdd:cd20620   18 HPDHIQHVLvtnARNYVKG-GVYERLKLLLGNGLLTSEGDLWRRQRRLAQPAFHRRRIAAYADAMVEATAALLDRWEAG- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 178 GQDSPLEVFQHVSLMTLDTIMKCAFShqgsIQVDRNSQSYIQAISDLNNLVFSRVRNAFHqndtiySLTSAGRWTHRACQ 257
Cdd:cd20620   96 ARRGPVDVHAEMMRLTLRIVAKTLFG----TDVEGEADEIGDALDVALEYAARRMLSPFL------LPLWLPTPANRRFR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 258 LAHQHTDQVIQLRKAQLQKEGElekikrkRHLDFLDILLLA-KMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYA 336
Cdd:cd20620  166 RARRRLDEVIYRLIAERRAAPA-------DGGDLLSMLLAArDEETGEPMSDQQLRDEVMTLFLAGHETTANALSWTWYL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 337 LATHPKHQERCREEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIY 416
Cdd:cd20620  239 LAQHPEVAARLRAEVDRVLGGRP-PTAEDLPQLPYTEMVLQESLRLYPPAWIIGREAVEDDEIGGYR-IPAGSTVLISPY 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 417 GLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARL 494
Cdd:cd20620  317 VTHRDPRFWPDPEAFDPERFTPEREAarPRYAYFPFGGGPRICIGNHFAMMEAVLLLATIAQRFRLRLVPGQPVEPEPLI 396
                        410
                 ....*....|
gi 158937242 495 VLKSKNGIHL 504
Cdd:cd20620  397 TLRPKNGVRM 406
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
90-502 9.54e-90

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: 282.03  E-value: 9.54e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  90 LWGGKVR-VQLYDPDYMKVILGRSD--PKSHgSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:cd20680   17 LWIGPVPfVILYHAENVEVILSSSKhiDKSY-LYKFLHPWLGTGLLTSTGEKWRSRRKMLTPTFHFTILSDFLEVMNEQS 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 167 RVMLDKWEELLGQDsPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQsYIQAISDLNNLVFSRVRNAFHQNDTIYSLT 246
Cdd:cd20680   96 NILVEKLEKHVDGE-AFNCFFDITLCALDIICETAMGKKIGAQSNKDSE-YVQAVYRMSDIIQRRQKMPWLWLDLWYLMF 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 247 SAGRWTHRACQLAHQHTDQVIQLRKAQLQKE--------GELEKiKRKRHLdFLDILLLAKMENGSILSDKDLRAEVDTF 318
Cdd:cd20680  174 KEGKEHNKNLKILHTFTDNVIAERAEEMKAEedktgdsdGESPS-KKKRKA-FLDMLLSVTDEEGNKLSHEDIREEVDTF 251
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 319 MFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPV 397
Cdd:cd20680  252 MFEGHDTTAAAMNWSLYLLGSHPEVQRKVHKELDEVFGKSdRPVTMEDLKKLRYLECVIKESLRLFPSVPLFARSLCEDC 331
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 398 TFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTL 475
Cdd:cd20680  332 EI-RGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFFPENSSgrHPYAYIPFSAGPRNCIGQRFALMEEKVVLSCIL 410
                        410       420
                 ....*....|....*....|....*...
gi 158937242 476 LRFELLPDPTRIPI-PIARLVLKSKNGI 502
Cdd:cd20680  411 RHFWVEANQKREELgLVGELILRPQNGI 438
CYP313-like cd11057
cytochrome P450 family 313 and similar cytochrome P450s; This subfamily is composed of insect ...
89-480 2.39e-88

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: 277.95  E-value: 2.39e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  89 WLwGGKVRVQLYDPDYMKVILGRSDPKSHGS-YRFLapWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11057    7 WL-GPRPFVITSDPEIVQVVLNSPHCLNKSFfYDFF--RLGRGLFSAPYPIWKLQRKALNPSFNPKILLSFLPIFNEEAQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 168 VMLDKWEELLGQDsPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSqSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTS 247
Cdd:cd11057   84 KLVQRLDTYVGGG-EFDILPDLSRCTLEMICQTTLGSDVNDESDGNE-EYLESYERLFELIAKRVLNPWLHPEFIYRLTG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 248 AGRWTHRACQLAHQHTDQVIQLRKAQLQKEGEL----EKIKRKRHLDFLDiLLLAKMENGSILSDKDLRAEVDTFMFEGH 323
Cdd:cd11057  162 DYKEEQKARKILRAFSEKIIEKKLQEVELESNLdseeDEENGRKPQIFID-QLLELARNGEEFTDEEIMDEIDTMIFAGN 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDG 402
Cdd:cd11057  241 DTSATTVAYTLLLLAMHPEVQEKVYEEIMEVFPDdGQFITYEDLQQLVYLEMVLKETMRLFPVGPLVGRETTADIQLSNG 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 403 RSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd11057  321 VVIPKGTTIVIDIFNMHRRKDIWgPDADQFDPDNFLPERSAqrHPYAFIPFSAGPRNCIGWRYAMISMKIMLAKILRNYR 400

                 .
gi 158937242 480 L 480
Cdd:cd11057  401 L 401
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
87-488 1.17e-85

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: 269.77  E-value: 1.17e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  87 PHWLWGGKVRVqLYDPDYMKVILGRSDPKSHGSYRFLA---PWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd00302    5 RVRLGGGPVVV-VSDPELVREVLRDPRDFSSDAGPGLPalgDFLGDGLLTLDGPEHRRLRRLLAPAFTPRALAALRPVIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 164 DSVRVMLDKWEELLGQDspLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRnsqsYIQAISDLNNLVFSRVRNAFhqndtiy 243
Cdd:cd00302   84 EIARELLDRLAAGGEVG--DDVADLAQPLALDVIARLLGGPDLGEDLEE----LAELLEALLKLLGPRLLRPL------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 244 sLTSAGRWTHRACQLAHQHTDQVIQLRkaqlqkegelekikRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGH 323
Cdd:cd00302  151 -PSPRLRRLRRARARLRDYLEELIARR--------------RAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLAGH 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGDGasiTWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGR 403
Cdd:cd00302  216 ETTASLLAWALYLLARHPEVQERLRAEIDAVLGDG---TPEDLSKLPYLEAVVEETLRLYPPVPLLPRVATEDVEL-GGY 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 404 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPD 483
Cdd:cd00302  292 TIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFLPEREEPRYAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELV 371

                 ....*
gi 158937242 484 PTRIP 488
Cdd:cd00302  372 PDEEL 376
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
130-502 1.60e-83

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: 265.22  E-value: 1.60e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 130 GLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQ 209
Cdd:cd11055   51 SLLFLKGERWKRLRTTLSPTFSSGKLKLMVPIINDCCDELVEKLEKAAETGKPVDMKDLFQGFTLDVILSTAFGIDVDSQ 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 210 VDRNSQSYIQAisdlnnlvfsrvRNAFHQNDTIYSLTSA-----------GRWTHRAcQLAH---QHTDQVIQLRKAQLQ 275
Cdd:cd11055  131 NNPDDPFLKAA------------KKIFRNSIIRLFLLLLlfplrlflfllFPFVFGF-KSFSfleDVVKKIIEQRRKNKS 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 276 kegelekikrKRHLDFLDILLLAK----MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 351
Cdd:cd11055  198 ----------SRRKDLLQLMLDAQdsdeDVSKKKLTDDEIVAQSFIFLLAGYETTSNTLSFASYLLATNPDVQEKLIEEI 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 352 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVF 431
Cdd:cd11055  268 DEVLPDDGSPTYDTVSKLKYLDMVINETLRLYPPAFFISRECKEDCTI-NGVFIPKGVDVVIPVYAIHHDPEFWPDPEKF 346
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158937242 432 DPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDP-TRIPIPI-ARLVLKSKNGI 502
Cdd:cd11055  347 DPERFSPENKAkrHPYAYLPFGAGPRNCIGMRFALLEVKLALVKILQKFRFVPCKeTEIPLKLvGGATLSPKNGI 421
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
97-506 6.99e-80

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: 255.59  E-value: 6.99e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  97 VQLYDPDYMKVILGRSDPKSHGSYRF--LAPWIG-YGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKW 173
Cdd:cd11053   26 VVLSDPEAIKQIFTADPDVLHPGEGNslLEPLLGpNSLLLLDGDRHRRRRKLLMPAFHGERLRAYGELIAEITEREIDRW 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 174 eellGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAIsDLNNLVFSRVRNAFHQNdtiysltsaGRWT- 252
Cdd:cd11053  106 ----PPGQPFDLRELMQEITLEVILRVVFGVDDGERLQELRRLLPRLL-DLLSSPLASFPALQRDL---------GPWSp 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 253 ----HRACQLAHQHTDQVIQLRKAQLQKEGElekikrkrhlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTAS 328
Cdd:cd11053  172 wgrfLRARRRIDALIYAEIAERRAEPDAERD----------DILSLLLSARDEDGQPLSDEELRDELMTLLFAGHETTAT 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 329 GISWILYALATHPKHQERCREEIHSLLGDGASitwNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKG 408
Cdd:cd11053  242 ALAWAFYWLHRHPEVLARLLAELDALGGDPDP---EDIAKLPYLDAVIKETLRLYPVAPLVPRRVKEPVEL-GGYTLPAG 317
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 409 IMVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRiP 488
Cdd:cd11053  318 TTVAPSIYLTHHRPDLYPDPERFRPERFL-GRKPSPYEYLPFGGGVRRCIGAAFALLEMKVVLATLLRRFRLELTDPR-P 395
                        410       420
                 ....*....|....*....|
gi 158937242 489 IPIAR--LVLKSKNGIHLRL 506
Cdd:cd11053  396 ERPVRrgVTLAPSRGVRMVV 415
CYP_FUM15-like cd11069
Fusarium verticillioides cytochrome P450 monooxygenase FUM15, and similar cytochrome P450s; ...
91-501 7.40e-79

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: 253.73  E-value: 7.40e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  91 WGGKVRVQLYDPDYMKVILGRSD---PKSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11069   10 LFGSERLLVTDPKALKHILVTNSydfEKPPAFRRLLRRILGDGLLAAEGEEHKRQRKILNPAFSYRHVKELYPIFWSKAE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 168 VMLDKWEELL----GQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQvdRNSQSYIQAISDL-----NNLVFSRVRNAFH 237
Cdd:cd11069   90 ELVDKLEEEIeesgDESISIDVLEWLSRATLDIIGLAGFGYDfDSLE--NPDNELAEAYRRLfeptlLGSLLFILLLFLP 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 238 QNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEgelekiKRKRHLDFLDILLLAKME-NGSILSDKDLRAEVD 316
Cdd:cd11069  168 RWLVRILPWKANREIRRAKDVLRRLAREIIREKKAALLEG------KDDSGKDILSILLRANDFaDDERLSDEELIDQIL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 317 TFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGD--GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELS 394
Cdd:cd11069  242 TFLAAGHETTSTALTWALYLLAKHPDVQERLREEIRAALPDppDGDLSYDDLDRLPYLNAVCRETLRLYPPVPLTSREAT 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 395 TPvTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF-------APGSAQHSHAFLPFSGGSRNCIGKQFAMNE 466
Cdd:cd11069  322 KD-TVIKGVPIPKGTVVLIPPAAINRSPEIWgPDAEEFNPERWlepdgaaSPGGAGSNYALLTFLHGPRSCIGKKFALAE 400
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 158937242 467 LKVATALTLLRFELLPDP-TRIPIPIARLVLKSKNG 501
Cdd:cd11069  401 MKVLLAALVSRFEFELDPdAEVERPIGIITRPPVDG 436
CYP72_clan cd11052
Plant cytochrome P450s, clan CYP72; CYPs have been classified into families and subfamilies ...
75-503 2.18e-76

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: 246.87  E-value: 2.18e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  75 IQKWVETFPSACPHWLwGGKVRVQLYDPDYMKVILGRSDPKSHGSY--RFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHY 152
Cdd:cd11052    4 YYHWIKQYGKNFLYWY-GTDPRLYVTEPELIKELLSKKEGYFGKSPlqPGLKKLLGRGLVMSNGEKWAKHRRIANPAFHG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 153 DILKPYVGLMADSVRVMLDKWEELLG-QDSPLEVFQHVSLMTLDTIMKCAF--SHQGSIQVDRNSQSYIQAISDLNNLVF 229
Cdd:cd11052   83 EKLKGMVPAMVESVSDMLERWKKQMGeEGEEVDVFEEFKALTADIISRTAFgsSYEEGKEVFKLLRELQKICAQANRDVG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 230 SRVRNAFHQNDTIysltsagrwthRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKRhlDFLDILLLA--KMENGSILS 307
Cdd:cd11052  163 IPGSRFLPTKGNK-----------KIKKLDKEIEDSLLEIIKKREDSLKMGRGDDYGD--DLLGLLLEAnqSDDQNKNMT 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 308 DKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGaSITWNHLDQMPYTTMCIKEALRLYPPVP 387
Cdd:cd11052  230 VQEIVDECKTFFFAGHETTALLLTWTTMLLAIHPEWQEKAREEVLEVCGKD-KPPSDSLSKLKTVSMVINESLRLYPPAV 308
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 388 GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPN-PEVFDPFRFAPGSAQ---HSHAFLPFSGGSRNCIGKQFA 463
Cdd:cd11052  309 FLTRKAKEDIKL-GGLVIPKGTSIWIPVLALHHDEEIWGEdANEFNPERFADGVAKaakHPMAFLPFGLGPRNCIGQNFA 387
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 158937242 464 MNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKNGIH 503
Cdd:cd11052  388 TMEAKIVLAMILQRFSFTLSPTYRHAPTVVLTLRPQYGLQ 427
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
131-503 1.01e-74

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: 242.44  E-value: 1.01e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 131 LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFShqgsiqV 210
Cdd:cd11056   53 LFSLDGEKWKELRQKLTPAFTSGKLKNMFPLMVEVGDELVDYLKKQAEKGKELEIKDLMARYTTDVIASCAFG------L 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 211 DRNSqsyiqaISDLNNLVFSRVRNAFHQNDTIY----SLTSAGRWTH--RACQLAHQHTD-------QVIQLRkaqlqke 277
Cdd:cd11056  127 DANS------LNDPENEFREMGRRLFEPSRLRGlkfmLLFFFPKLARllRLKFFPKEVEDffrklvrDTIEYR------- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 278 gELEKIKRKrhlDFLDILL-------LAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE 350
Cdd:cd11056  194 -EKNNIVRN---DFIDLLLelkkkgkIEDDKSEKELTDEELAAQAFVFFLAGFETSSSTLSFALYELAKNPEIQEKLREE 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 351 IHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNP 428
Cdd:cd11056  270 IDEVLEKhGGELTYEALQEMKYLDQVVNETLRKYPPLPFLDRVCTKDYTLPGTDvVIEKGTPVIIPVYALHHDPKYYPEP 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 429 EVFDPFRFAPG--SAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDP-TRIPIPI--ARLVLKSKNGIH 503
Cdd:cd11056  350 EKFDPERFSPEnkKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPSSkTKIPLKLspKSFVLSPKGGIW 429
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
92-502 3.61e-73

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: 238.80  E-value: 3.61e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  92 GGKVRVQLYDPDYMKVILgRSDPKSHGSYRFLA----PWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVR 167
Cdd:cd11046   19 GPKSFLVISDPAIAKHVL-RSNAFSYDKKGLLAeilePIMGKGLIPADGEIWKKRRRALVPALHKDYLEMMVRVFGRCSE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 168 VMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQvdrNSQSYIQAisdlnnlVFSRVRNAFHQN------- 239
Cdd:cd11046   98 RLMEKLDAAAETGESVDMEEEFSSLTLDIIGLAVFNYDfGSVT---EESPVIKA-------VYLPLVEAEHRSvweppyw 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 240 DTIYSLTSAGRWTH--RACQLAHQHTDQVIQLRKAQLQKEgELEKIKRKR-HLDFLDILLLAKMENGSILSDKDLRAEVD 316
Cdd:cd11046  168 DIPAALFIVPRQRKflRDLKLLNDTLDDLIRKRKEMRQEE-DIELQQEDYlNEDDPSLLRFLVDMRDEDVDSKQLRDDLM 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 317 TFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTP 396
Cdd:cd11046  247 TMLIAGHETTAAVLTWTLYELSQNPELMAKVQAEVDAVLGDRLPPTYEDLKKLKYTRRVLNESLRLYPQPPVLIRRAVED 326
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 397 VTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH------AFLPFSGGSRNCIGKQFAMNELKV 469
Cdd:cd11046  327 DKLPGGGvKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNeviddfAFLPFGGGPRKCLGDQFALLEATV 406
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 158937242 470 ATALTLLRFELLPDPTRIPI---PIARLVlkSKNGI 502
Cdd:cd11046  407 ALAMLLRRFDFELDVGPRHVgmtTGATIH--TKNGL 440
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
75-502 2.65e-69

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: 228.17  E-value: 2.65e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  75 IQKWVETFPSACPHWLWGgKVRVQLYDPDYMKVILGRSD-PKSHGSYRFLA-----PWIGYGLL-LLNGQTWFQHRRMLT 147
Cdd:cd20613    4 LLEWAKEYGPVFVFWILH-RPIVVVSDPEAVKEVLITLNlPKPPRVYSRLAflfgeRFLGNGLVtEVDHEKWKKRRAILN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 148 PAFHYDILKpyvGLMA---DSVRVMLDKWEELlgQDSPLEV--FQHVSLMTLDTIMKCAFSHQGSIQVDRNSQsYIQAIS 222
Cdd:cd20613   83 PAFHRKYLK---NLMDefnESADLLVEKLSKK--ADGKTEVnmLDEFNRVTLDVIAKVAFGMDLNSIEDPDSP-FPKAIS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 223 D-LNNLVFSRvRNAFHQndtiysLTSAGRWTHR----ACQLAHQHTDQVIQLRKAQLQKEGELEKikrkrhldflDIL-- 295
Cdd:cd20613  157 LvLEGIQESF-RNPLLK------YNPSKRKYRRevreAIKFLRETGRECIEERLEALKRGEEVPN----------DILth 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 296 LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMC 375
Cdd:cd20613  220 ILKASEEEPDFDMEELLDDFVTFFIAGQETTANLLSFTLLELGRHPEILKRLQAEVDEVLGSKQYVEYEDLGKLEYLSQV 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 376 IKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGS--AQHSHAFLPFSGG 453
Cdd:cd20613  300 LKETLRLYPPVPGTSRELTKDIEL-GGYKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEApeKIPSYAYFPFSLG 378
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158937242 454 SRNCIGKQFAMNELKVATA--LTLLRFELLPDPTRipIPIARLVLKSKNGI 502
Cdd:cd20613  379 PRSCIGQQFAQIEAKVILAklLQNFKFELVPGQSF--GILEEVTLRPKDGV 427
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
120-507 1.80e-63

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: 212.50  E-value: 1.80e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 120 YRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllGQdsPLEVFQHVSLMTLDTIMK 199
Cdd:cd11049   51 FDRARPLLGNGLATCPGEDHRRQRRLMQPAFHRSRIPAYAEVMREEAEALAGSWRP--GR--VVDVDAEMHRLTLRVVAR 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 200 CAFSHQGSiqvDRNSQSYIQAISDLNNLVFSRvrnafhqndTIY--SL----TSAGRWTHRACQLAHQHTDQVIQLRKAQ 273
Cdd:cd11049  127 TLFSTDLG---PEAAAELRQALPVVLAGMLRR---------AVPpkFLerlpTPGNRRFDRALARLRELVDEIIAEYRAS 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 274 LQKEGelekikrkrhlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHS 353
Cdd:cd11049  195 GTDRD-----------DLLSLLLAARDEEGRPLSDEELRDQVITLLTAGTETTASTLAWAFHLLARHPEVERRLHAELDA 263
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 354 LLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDP 433
Cdd:cd11049  264 VLG-GRPATFEDLPRLTYTRRVVTEALRLYPPVWLLTRRTTADVEL-GGHRLPAGTEVAFSPYALHRDPEVYPDPERFDP 341
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158937242 434 FRFAPG--SAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKngiHLRLR 507
Cdd:cd11049  342 DRWLPGraAAVPRGAFIPFGAGARKCIGDTFALTELTLALATIASRWRLRPVPGRPVRPRPLATLRPR---RLRMR 414
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
111-508 2.11e-62

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


Pssm-ID: 410691 [Multi-domain]  Cd Length: 430  Bit Score: 210.12  E-value: 2.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 111 RSDPKSHGSYRFLAPWIGYGLLLLNG--QTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELlGQDSPLEVFQH 188
Cdd:cd11068   42 RFDKKVSGPLEELRDFAGDGLFTAYThePNWGKAHRILMPAFGPLAMRGYFPMMLDIAEQLVLKWERL-GPDEPIDVPDD 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 189 VSLMTLDTIMKCAFSHQ-GSIQVDRnSQSYIQAISDLNNLVFSRVRNAFHQNDTiysLTSAGRWTHRACQLAHQHTDQVI 267
Cdd:cd11068  121 MTRLTLDTIALCGFGYRfNSFYRDE-PHPFVEAMVRALTEAGRRANRPPILNKL---RRRAKRQFREDIALMRDLVDEII 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 268 QLRKAQlqkegelekiKRKRHLDFLDILLLAK-MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 346
Cdd:cd11068  197 AERRAN----------PDGSPDDLLNLMLNGKdPETGEKLSDENIRYQMITFLIAGHETTSGLLSFALYYLLKNPEVLAK 266
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 347 CREEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW- 425
Cdd:cd11068  267 ARAEVDEVLGDDP-PPYEQVAKLRYIRRVLDETLRLWPTAPAFARKPKEDTVLGGKYPLKKGDPVLVLLPALHRDPSVWg 345
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 426 PNPEVFDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPtRIPIPIA-RLVLKSKnGI 502
Cdd:cd11068  346 EDAEEFRPERFLPEEFRklPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFEDDP-DYELDIKeTLTLKPD-GF 423

                 ....*.
gi 158937242 503 HLRLRR 508
Cdd:cd11068  424 RLKARP 429
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
97-480 1.80e-61

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: 207.76  E-value: 1.80e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  97 VQLYDPDYMKVILgRSDPKsHGSYRFLAPWIGY--------GLLLLNGQTWFQHRRMLTPafhyDILKP-----YVGLMA 163
Cdd:cd11054   18 VHLFDPDDIEKVF-RNEGK-YPIRPSLEPLEKYrkkrgkplGLLNSNGEEWHRLRSAVQK----PLLRPksvasYLPAIN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 164 DSVRVMLDKWEELLGQDS--PLEVFQHVSLMTLDTIMKCAF-SHQGSIQVDRNS--QSYIQAISDLNNLVfsrvrnafhq 238
Cdd:cd11054   92 EVADDFVERIRRLRDEDGeeVPDLEDELYKWSLESIGTVLFgKRLGCLDDNPDSdaQKLIEAVKDIFESS---------- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 239 NDTIYSLTSAGRW-THRACQLAhQHTDQVIQLRKAQLQKEgeLEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDT 317
Cdd:cd11054  162 AKLMFGPPLWKYFpTPAWKKFV-KAWDTIFDIASKYVDEA--LEELKKKDEEDEEEDSLLEYLLSKPGLSKKEIVTMALD 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 318 FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPV 397
Cdd:cd11054  239 LLLAGVDTTSNTLAFLLYHLAKNPEVQEKLYEEIRSVLPDGEPITAEDLKKMPYLKACIKESLRLYPVAPGNGRILPKDI 318
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 398 TFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF----APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATAL 473
Cdd:cd11054  319 VL-SGYHIPKGTLVVLSNYVMGRDEEYFPDPEEFIPERWlrddSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAK 397

                 ....*..
gi 158937242 474 TLLRFEL 480
Cdd:cd11054  398 LLQNFKV 404
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
90-483 2.41e-60

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: 204.37  E-value: 2.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  90 LWGGKVR-VQLYDPDYMKVIL--------GRSDPKSHGSYRFlapwiGYGLLLLNGQTWFQHRRMLTPAF--HYDILKPY 158
Cdd:cd20617    6 LWLGDVPtVVLSDPEIIKEAFvkngdnfsDRPLLPSFEIISG-----GKGILFSNGDYWKELRRFALSSLtkTKLKKKME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 159 vGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLV-FSRVRNAFH 237
Cdd:cd20617   81 -ELIEEEVNKLIESLKKHSKSGEPFDPRPYFKKFVLNIINQFLFGKRFPDEDDGEFLKLVKPIEEIFKELgSGNPSDFIP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 238 QNDTIYSLTSagRWTHRACQLAHQHTDQVIQLRKAQLQKEGElekikrkRHLDFLDILLLAKMENGSILSDKDLRAEVDT 317
Cdd:cd20617  160 ILLPFYFLYL--KKLKKSYDKIKDFIEKIIEEHLKTIDPNNP-------RDLIDDELLLLLKEGDSGLFDDDSIISTCLD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 318 FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTP 396
Cdd:cd20617  231 LFLAGTDTTSTTLEWFLLYLANNPEIQEKIYEEIDNVVGNDRRVTLSDRSKLPYLNAVIKEVLRLRPILPlGLPRVTTED 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 397 VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTL 475
Cdd:cd20617  311 TEI-GGYFIPKGTQIIINIYSLHRDEKYFEDPEEFNPERFlENDGNKLSEQFIPFGIGKRNCVGENLARDELFLFFANLL 389

                 ....*...
gi 158937242 476 LRFELLPD 483
Cdd:cd20617  390 LNFKFKSS 397
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
88-508 3.71e-60

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: 203.59  E-value: 3.71e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  88 HWLWGGKVR-VQLYDPDYMKVILGRSD--PKSHGSYRFLAP--WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLM 162
Cdd:COG2124   35 FRVRLPGGGaWLVTRYEDVREVLRDPRtfSSDGGLPEVLRPlpLLGDSLLTLDGPEHTRLRRLVQPAFTPRRVAALRPRI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 163 ADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQGSiqvDRNSqsyiqaisdlnnlvFSRVRNAFHQNDTI 242
Cdd:COG2124  115 REIADELLDRLAA----RGPVDLVEEFARPLPVIVICELLGVPEE---DRDR--------------LRRWSDALLDALGP 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 243 YSLTSAGRwTHRACQLAHQHTDQVIQLRKAQLQKegelekikrkrhlDFLDILLLAKmENGSILSDKDLRAEVDTFMFEG 322
Cdd:COG2124  174 LPPERRRR-ARRARAELDAYLRELIAERRAEPGD-------------DLLSALLAAR-DDGERLSDEELRDELLLLLLAG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 323 HDTTASGISWILYALATHPKHQERCREEIhsllgdgasitwnhldqmPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDG 402
Cdd:COG2124  239 HETTANALAWALYALLRHPEQLARLRAEP------------------ELLPAAVEETLRLYPPVPLLPRTATEDVEL-GG 299
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 403 RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsaqHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELL- 481
Cdd:COG2124  300 VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR-------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFPDLr 372
                        410       420
                 ....*....|....*....|....*..
gi 158937242 482 PDPTRIPIPIARLVLKSKNGIHLRLRR 508
Cdd:COG2124  373 LAPPEELRWRPSLTLRGPKSLPVRLRP 399
CYP734 cd20639
cytochrome P450 family 734; Cytochrome P450 family 734 (CYP734) belongs to the plant CYP72 ...
87-503 2.37e-59

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: 202.29  E-value: 2.37e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  87 PHWLW-GGKVRVQLYDPDYMK-VILGRSDP-KSHGSYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd20639   14 TFLYWfGPTPRLTVADPELIReILLTRADHfDRYEAHPLVRQLEGDGLVSLRGEKWAHHRRVITPAFHMENLKRLVPHVV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 164 DSVRVMLDKWEELLGQDSPLEV-----FQHVslmTLDTIMKCAFshqGSiqvdrnsqSYIQAisdlnnlvfsrvRNAFHQ 238
Cdd:cd20639   94 KSVADMLDKWEAMAEAGGEGEVdvaewFQNL---TEDVISRTAF---GS--------SYEDG------------KAVFRL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 239 NDTIYSLTSAGRWT--------------HRACQLAHQ---HTDQVIQLRKAQLQKEGELEKIKrkrhlDFLDILLLAK-M 300
Cdd:cd20639  148 QAQQMLLAAEAFRKvyipgyrflptkknRKSWRLDKEirkSLLKLIERRQTAADDEKDDEDSK-----DLLGLMISAKnA 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 301 ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEAL 380
Cdd:cd20639  223 RNGEKMTVEEIIEECKTFFFAGKETTSNLLTWTTVLLAMHPEWQERARREVLAVCGKGDVPTKDHLPKLKTLGMILNETL 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 381 RLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGS---AQHSHAFLPFSGGSRN 456
Cdd:cd20639  303 RLYPPAVATIRRAKKDVKL-GGLDIPAGTELLIPIMAIHHDAELWgNDAAEFNPARFADGVaraAKHPLAFIPFGLGPRT 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 158937242 457 CIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKNGIH 503
Cdd:cd20639  382 CVGQNLAILEAKLTLAVILQRFEFRLSPSYAHAPTVLMLLQPQHGAP 428
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
126-493 1.12e-58

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: 200.20  E-value: 1.12e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 126 WIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQ 205
Cdd:cd11044   66 LGENSLSLQDGEEHRRRRKLLAPAFSREALESYVPTIQAIVQSYLRKWLK----AGEVALYPELRRLTFDVAARLLLGLD 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 206 GSIQVDRNSQSYIQAISDLN----NLVFSRVRNAFhqndtiysltsagrwthRACQLAHQHTDQVIQLRKAQLQKEGele 281
Cdd:cd11044  142 PEVEAEALSQDFETWTDGLFslpvPLPFTPFGRAI-----------------RARNKLLARLEQAIRERQEEENAEA--- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 282 kikrkrhLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAsI 361
Cdd:cd11044  202 -------KDALGLLLEAKDEDGEPLSMDELKDQALLLLFAGHETTASALTSLCFELAQHPDVLEKLRQEQDALGLEEP-L 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 362 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAP-GS 440
Cdd:cd11044  274 TLESLKKMPYLDQVIKEVLRLVPPVGGGFRKVLEDFEL-GGYQIPKGWLVYYSIRDTHRDPELYPDPERFDPERFSPaRS 352
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 441 AQHSHAF--LPFSGGSRNCIGKQFAMNELKVATAlTLLR---FELLP--DPTRIPIPIAR 493
Cdd:cd11044  353 EDKKKPFslIPFGGGPRECLGKEFAQLEMKILAS-ELLRnydWELLPnqDLEPVVVPTPR 411
CYP714 cd20640
cytochrome P450 family 714; Cytochrome P450 family 714 (CYP714) belongs to the plant CYP72 ...
77-504 8.12e-57

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: 195.32  E-value: 8.12e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  77 KWVETFPSACPHWLwGGKVRVQLYDPDYMKVI-------LGRSD--PKSHGsyrflaPWIGYGLLLLNGQTWFQHRRMLT 147
Cdd:cd20640    6 KWRKQYGPIFTYST-GNKQFLYVSRPEMVKEInlcvsldLGKPSylKKTLK------PLFGGGILTSNGPHWAHQRKIIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 148 PAFHYDILKPYVGLMADSVRVMLDKWEELL----GQDSPLEVFQHVSLMTLDTIMKCAFshqGSiqvdrnsqSYIQAISd 223
Cdd:cd20640   79 PEFFLDKVKGMVDLMVDSAQPLLSSWEERIdragGMAADIVVDEDLRAFSADVISRACF---GS--------SYSKGKE- 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 224 lnnlVFSRVRN---AFHQNDTIYSLTSAgRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIKRKrhlDFLDILLLAKM 300
Cdd:cd20640  147 ----IFSKLRElqkAVSKQSVLFSIPGL-RHLPTKSNRKIWELEGEIRSLILEIVKEREEECDHEK---DLLQAILEGAR 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 301 engsilSDKDLRAEVDTFM--------FEGHDTTASGISWILYALATHPKHQERCREEIHSLLGdGASITWNHLDQMPYT 372
Cdd:cd20640  219 ------SSCDKKAEAEDFIvdnckniyFAGHETTAVTAAWCLMLLALHPEWQDRVRAEVLEVCK-GGPPDADSLSRMKTV 291
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 373 TMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFA---PGSAQHSHAFL 448
Cdd:cd20640  292 TMVIQETLRLYPPAAFVSREALRDMKLGGLV-VPKGVNIWVPVSTLHLDPEIWgPDANEFNPERFSngvAAACKPPHSYM 370
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 158937242 449 PFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKNGIHL 504
Cdd:cd20640  371 PFGAGARTCLGQNFAMAELKVLVSLILSKFSFTLSPEYQHSPAFRLIVEPEFGVRL 426
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
140-484 8.13e-56

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: 192.43  E-value: 8.13e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 140 FQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeellGQDSPLEVFQHVSLMTLDTIMKCAfshQGSiqvdrnsqsyiq 219
Cdd:cd11042   65 KEQLKFGLNILRRGKLRGYVPLIVEEVEKYFAKW----GESGEVDLFEEMSELTILTASRCL---LGK------------ 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 220 aisDLNNLVFSRVRNAFHQNDTIYSLTSAGRW-----THRACQLAHQHTD----QVIQLRKAQLQKEGelekikrkrhLD 290
Cdd:cd11042  126 ---EVRELLDDEFAQLYHDLDGGFTPIAFFFPplplpSFRRRDRARAKLKeifsEIIQKRRKSPDKDE----------DD 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 291 FLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGD-GASITWNHLDQM 369
Cdd:cd11042  193 MLQTLMDAKYKDGRPLTDDEIAGLLIALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDgDDPLTYDVLKEM 272
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 370 PYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR-SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH--- 445
Cdd:cd11042  273 PLLHACIKETLRLHPPIHSLMRKARKPFEVEGGGyVIPKGHIVLASPAVSHRDPEIFKNPDEFDPERFLKGRAEDSKggk 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 158937242 446 -AFLPFSGGSRNCIGKQFAMNELKV--ATALTLLRFELLPDP 484
Cdd:cd11042  353 fAYLPFGAGRHRCIGENFAYLQIKTilSTLLRNFDFELVDSP 394
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
92-484 7.48e-55

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: 190.16  E-value: 7.48e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  92 GGKVRVQLYDPDYMKVILgrsdpKSHGSYRFLAPWIGY------GLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADS 165
Cdd:cd20621   11 GSKPLISLVDPEYIKEFL-----QNHHYYKKKFGPLGIdrlfgkGLLFSEGEEWKKQRKLLSNSFHFEKLKSRLPMINEI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 166 VRVMLDKWEELLGQdspleVFQHVSLMTLDTIMKCAFS--------HQGSIQVDRNSQSYIQAISDLNNLVFSRVRNAFH 237
Cdd:cd20621   86 TKEKIKKLDNQNVN-----IIQFLQKITGEVVIRSFFGeeakdlkiNGKEIQVELVEILIESFLYRFSSPYFQLKRLIFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 238 QNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEgeleKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDT 317
Cdd:cd20621  161 RKSWKLFPTKKEKKLQKRVKELRQFIEKIIQNRIKQIKKN----KDEIKDIIIDLDLYLLQKKKLEQEITKEEIIQQFIT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 318 FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPG-IGRELSTP 396
Cdd:cd20621  237 FFFAGTDTTGHLVGMCLYYLAKYPEIQEKLRQEIKSVVGNDDDITFEDLQKLNYLNAFIKEVLRLYNPAPFlFPRVATQD 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 397 VTFPDgRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALT 474
Cdd:cd20621  317 HQIGD-LKIKKGWIVNVGYIYNHFNPKYFENPDEFNPERWlnQNNIEDNPFVFIPFSAGPRNCIGQHLALMEAKIILIYI 395
                        410
                 ....*....|
gi 158937242 475 LLRFELLPDP 484
Cdd:cd20621  396 LKNFEIEIIP 405
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
89-491 3.29e-54

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: 187.91  E-value: 3.29e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  89 WLWGGKVR-VQLYDPDYMKVILgRSDPKSHGSYR----FLAPWIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd11045   15 WTGMLGLRvVALLGPDANQLVL-RNRDKAFSSKQgwdpVIGPFFHRGLMLLDFDEHRAHRRIMQQAFTRSALAGYLDRMT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 164 DSVRVMLDKWEEllgqDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQAISDLNNLVFSRVrnafhqndtiy 243
Cdd:cd11045   94 PGIERALARWPT----GAGFQFYPAIKELTLDLATRVFLGVDLGPEADKVNKAFIDTVRASTAIIRTPI----------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 244 sltSAGRWtHRAcqlahqhtdqviqLRKAQLQKEGELEKIKRKRHL---DFLDILLLAKMENGSILSDKDLRAEVDTFMF 320
Cdd:cd11045  159 ---PGTRW-WRG-------------LRGRRYLEEYFRRRIPERRAGggdDLFSALCRAEDEDGDRFSDDDIVNHMIFLMM 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 321 EGHDTTASGISWILYALATHPKHQERCREEIHSLlGDGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFp 400
Cdd:cd11045  222 AAHDTTTSTLTSMAYFLARHPEWQERLREESLAL-GKGT-LDYEDLGQLEVTDWVFKEALRLVPPVPTLPRRAVKDTEV- 298
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 401 DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA---QHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLR 477
Cdd:cd11045  299 LGYRIPAGTLVAVSPGVTHYMPEYWPNPERFDPERFSPERAedkVHRYAWAPFGGGAHKCIGLHFAGMEVKAILHQMLRR 378
                        410       420
                 ....*....|....*....|
gi 158937242 478 FELL------PDPTRIPIPI 491
Cdd:cd11045  379 FRWWsvpgyyPPWWQSPLPA 398
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
101-479 1.10e-53

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: 186.74  E-value: 1.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 101 DPDYMKVILGRSDPKSHG-SYRFLAPWIGYGLL-LLNGQTWFQHRRMLTPAFHydilKPYVGL------MADSVRVMLDK 172
Cdd:cd11059   15 DLDAVREIYGGGFGKTKSyWYFTLRGGGGPNLFsTLDPKEHSARRRLLSGVYS----KSSLLRaamepiIRERVLPLIDR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 173 WEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYiqaisdlnnlvfSRVRNAFHQNDTIYSLTSAGRWT 252
Cdd:cd11059   91 IAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGTLLLGDKDSR------------ERELLRRLLASLAPWLRWLPRYL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 253 HRA--------CQLAHQHTDQ-VIQLRKAQLQKEGELEKIKRKRHLDFLDilllAKMENGSILSDKDLRAEVDTFMFEGH 323
Cdd:cd11059  159 PLAtsrliigiYFRAFDEIEEwALDLCARAESSLAESSDSESLTVLLLEK----LKGLKKQGLDDLEIASEALDHIVAGH 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIG-RELSTPVTFPD 401
Cdd:cd11059  235 DTTAVTLTYLIWELSRPPNLQEKLREELAGLPGPfRGPPDLEDLDKLPYLNAVIRETLRLYPPIPGSLpRVVPEGGATIG 314
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 402 GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH----AFLPFSGGSRNCIGKQFAMNELKVATALTLLR 477
Cdd:cd11059  315 GYYIPGGTIVSTQAYSLHRDPEVFPDPEEFDPERWLDPSGETARemkrAFWPFGSGSRMCIGMNLALMEMKLALAAIYRN 394

                 ..
gi 158937242 478 FE 479
Cdd:cd11059  395 YR 396
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
97-486 4.24e-53

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: 185.61  E-value: 4.24e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  97 VQLYDPDYMKVILGRSD--PKSHGSYRFLAPwigYG--LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDK 172
Cdd:cd11070   15 ILVTKPEYLTQIFRRRDdfPKPGNQYKIPAF---YGpnVISSEGEDWKRYRKIVAPAFNERNNALVWEESIRQAQRLIRY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 173 WEE--LLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQvDRNSQSYIQAISDLNNLVFSRVRNAFhqndTIYSLTsaGR 250
Cdd:cd11070   92 LLEeqPSAKGGGVDVRDLLQRLALNVIGEVGFGFDLPAL-DEEESSLHDTLNAIKLAIFPPLFLNF----PFLDRL--PW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 251 WTHRACQLAHQhtdQVIQLRKAqLQKEGELEKIKRKRHLDFLDILL---LAKMENGSILSDKDLRAEVDTFMFEGHDTTA 327
Cdd:cd11070  165 VLFPSRKRAFK---DVDEFLSE-LLDEVEAELSADSKGKQGTESVVasrLKRARRSGGLTEKELLGNLFIFFIAGHETTA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 328 SGISWILYALATHPKHQERCREEIHSLLGDGASITWNH--LDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRS- 404
Cdd:cd11070  241 NTLSFALYLLAKHPEVQDWLREEIDSVLGDEPDDWDYEedFPKLPYLLAVIYETLRLYPPVQLLNRKTTEPVVVITGLGq 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 405 ---LPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGS-----AQHSH----AFLPFSGGSRNCIGKQFAMNELKVAT 471
Cdd:cd11070  321 eivIPKGTYVGYNAYATHRDPTIWgPDADEFDPERWGSTSgeigaATRFTpargAFIPFSAGPRACLGRKFALVEFVAAL 400
                        410
                 ....*....|....*
gi 158937242 472 ALTLLRFELLPDPTR 486
Cdd:cd11070  401 AELFRQYEWRVDPEW 415
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
112-479 6.91e-53

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: 184.38  E-value: 6.91e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 112 SDPKSHGSYRFLAPWIG-YGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVS 190
Cdd:cd11051   29 NLPKPPPLRKFLTPLTGgSSLISMEGEEWKRLRKRFNPGFSPQHLMTLVPTILDEVEIFAAILRELAESGEVFSLEELTT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 191 LMTLDTIMKCAFShqgsiqVDRNSQSYIQAISDLNNLVFSRVRNAFHqndtIYSLTSAGRWthracqlahqhtdqviqLR 270
Cdd:cd11051  109 NLTFDVIGRVTLD------IDLHAQTGDNSLLTALRLLLALYRSLLN----PFKRLNPLRP-----------------LR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 271 KAQLQK--EGELEKIKRKRHLdfLDILLlakmengsilsdkdlrAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 348
Cdd:cd11051  162 RWRNGRrlDRYLKPEVRKRFE--LERAI----------------DQIKTFLFAGHDTTSSTLCWAFYLLSKHPEVLAKVR 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 349 EEIHSLLGDGASITW-------NHLDQMPYTTMCIKEALRLYPPV-------PGIGrelstpVTFPDGRSLP-KGIMVLL 413
Cdd:cd11051  224 AEHDEVFGPDPSAAAellregpELLNQLPYTTAVIKETLRLFPPAgtarrgpPGVG------LTDRDGKEYPtDGCIVYV 297
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 414 SIYGLHHNPKVWPNPEVFDPFRF--APGSAQH--SHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd11051  298 CHHAIHRDPEYWPRPDEFIPERWlvDEGHELYppKSAWRPFERGPRNCIGQELAMLELKIILAMTVRRFD 367
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
128-501 2.52e-52

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: 183.56  E-value: 2.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 128 GYGLLLLNGQTWFQHRRMLTPAFHydiLKPYVGLMADSVRvmlDKWEELL--------GQDSPLEvFQHVSL-MTLDTIM 198
Cdd:cd11064   48 GDGIFNVDGELWKFQRKTASHEFS---SRALREFMESVVR---EKVEKLLvplldhaaESGKVVD-LQDVLQrFTFDVIC 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 199 KCAFSHQ-GSIQVDRNSQSYIQAISDLNNLVFSRvrnaFHQNDTIYSLTsagRWTH--------RACQLAHQHTDQVIQL 269
Cdd:cd11064  121 KIAFGVDpGSLSPSLPEVPFAKAFDDASEAVAKR----FIVPPWLWKLK---RWLNigsekklrEAIRVIDDFVYEVISR 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 270 RKAQLQKEGElekiKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCRE 349
Cdd:cd11064  194 RREELNSREE----ENNVREDLLSRFLASEEEEGEPVSDKFLRDIVLNFILAGRDTTAAALTWFFWLLSKNPRVEEKIRE 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 350 EIHSLLGDGASITW-----NHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKV 424
Cdd:cd11064  270 ELKSKLPKLTTDESrvptyEELKKLVYLHAALSESLRLYPPVPFDSKEAVNDDVLPDGTFVKKGTRIVYSIYAMGRMESI 349
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 425 W-PNPEVFDPFRF--APGSAQH--SHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSK 499
Cdd:cd11064  350 WgEDALEFKPERWldEDGGLRPesPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVEPKMSLTLHMK 429

                 ..
gi 158937242 500 NG 501
Cdd:cd11064  430 GG 431
CYP709 cd20641
cytochrome P450 family 709; Cytochrome P450 family 709 (CYP709) belongs to the plant CYP72 ...
76-502 3.87e-52

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: 183.03  E-value: 3.87e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  76 QKWVETFPSACPHWLwGGKVRVQLYDPDYMKVILgrSDPKSHGSYRFLAPWI----GYGLLLLNGQTWFQHRRMLTPAFH 151
Cdd:cd20641    5 QQWKSQYGETFLYWQ-GTTPRICISDHELAKQVL--SDKFGFFGKSKARPEIlklsGKGLVFVNGDDWVRHRRVLNPAFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 152 YDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSL----MTLDTIMKCAF--SHQGSIQVDRnSQSYIQ--AISD 223
Cdd:cd20641   82 MDKLKSMTQVMADCTERMFQEWRKQRNNSETERIEVEVSRefqdLTADIIATTAFgsSYAEGIEVFL-SQLELQkcAAAS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 224 LNNLVFSrvrnafhqnDTIYSLTSAGRwthRACQLAHQHTDQVIQLRKAQLQKEGelekikRKRHLDFLDILLLAKMENG 303
Cdd:cd20641  161 LTNLYIP---------GTQYLPTPRNL---RVWKLEKKVRNSIKRIIDSRLTSEG------KGYGDDLLGLMLEAASSNE 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 304 S------ILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIK 377
Cdd:cd20641  223 GgrrterKMSIDEIIDECKTFFFAGHETTSNLLTWTMFLLSLHPDWQEKLREEVFRECGKDKIPDADTLSKLKLMNMVLM 302
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 378 EALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPG---SAQHSHAFLPFSGG 453
Cdd:cd20641  303 ETLRLYGPVINIARRASEDMKL-GGLEIPKGTTIIIPIAKLHRDKEVWgSDADEFNPLRFANGvsrAATHPNALLSFSLG 381
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 158937242 454 SRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARLVLKSKNGI 502
Cdd:cd20641  382 PRACIGQNFAMIEAKTVLAMILQRFSFSLSPEYVHAPADHLTLQPQYGL 430
CYP52 cd11063
cytochrome P450 family 52; Cytochrome P450 52 (CYP52), also called P450ALK, monooxygenases ...
101-501 5.13e-52

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: 182.37  E-value: 5.13e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 101 DPDYMKVILG-RSDPKSHGSYR--FLAPWIGYGLLLLNGQTWFQHRRMLTPAF------HYDILKPYVGLMADSVRvmld 171
Cdd:cd11063   19 EPENIKAVLAtQFKDFGLGERRrdAFKPLLGDGIFTSDGEEWKHSRALLRPQFsrdqisDLELFERHVQNLIKLLP---- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 172 kweellGQDSPLEVFQHVSLMTLDTIMKCAFSHqgSIQVDRNSQSYI------QAISDLNNLVFSRVRNafhqnDTIYSL 245
Cdd:cd11063   95 ------RDGSTVDLQDLFFRLTLDSATEFLFGE--SVDSLKPGGDSPpaarfaEAFDYAQKYLAKRLRL-----GKLLWL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 246 TSAGRWtHRACQLAHQHTDQVIQlrKAQLQKEGELEKIKRKRhldflDILLLAKMENGSilSDKDLRAEVDTFMFEGHDT 325
Cdd:cd11063  162 LRDKKF-REACKVVHRFVDPYVD--KALARKEESKDEESSDR-----YVFLDELAKETR--DPKELRDQLLNILLAGRDT 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 326 TASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFP----- 400
Cdd:cd11063  232 TASLLSFLFYELARHPEVWAKLREEVLSLFGPEPTPTYEDLKNMKYLRAVINETLRLYPPVPLNSRVAVRDTTLPrgggp 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 401 DGRS---LPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSaQHSHAFLPFSGGSRNCIGKQFAMNElkvaTALTLL 476
Cdd:cd11063  312 DGKSpifVPKGTRVLYSVYAMHRRKDIWgPDAEEFRPERWEDLK-RPGWEYLPFNGGPRICLGQQFALTE----ASYVLV 386
                        410       420       430
                 ....*....|....*....|....*....|
gi 158937242 477 RF-----ELLPDPTRIPIPIARLVLKSKNG 501
Cdd:cd11063  387 RLlqtfdRIESRDVRPPEERLTLTLSNANG 416
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
129-508 1.49e-51

plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, cytochrome P450 family 90, subfamily B, polypeptide 1, and cytochrome P450 family 90, subfamily D, polypeptide 2; This family is composed of plant cytochrome P450s including: Arabidopsis thaliana cytochrome P450s 85A1 (CYP85A1 or brassinosteroid-6-oxidase 1), 90A1 (CYP90A1), 88A3 (CYP88A3 or ent-kaurenoic acid oxidase 1), 90B1 (CYP90B1 or Dwarf4 or steroid 22-alpha-hydroxylase), and 90C1 (CYP90C1 or 3-epi-6-deoxocathasterone 23-monooxygenase); Oryza sativa cytochrome P450s 90D2 (CYP90D2 or C6-oxidase), 87A3 (CYP87A3), and 724B1 (CYP724B1 or dwarf protein 11); and Taxus cuspidata cytochrome P450 725A2 (CYP725A2 or taxane 13-alpha-hydroxylase). These enzymes are monooxygenases that catalyze oxidation reactions involved in steroid or hormone biosynthesis. CYP85A1, CYP90D2, and CYP90C1 are involved in brassinosteroids biosynthesis, while CYP88A3 catalyzes three successive oxidations of ent-kaurenoic acid, which is a key step in the synthesis of gibberellins. This family belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410669 [Multi-domain]  Cd Length: 408  Bit Score: 180.84  E-value: 1.49e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 129 YGLLLLNGqtwFQHRRM---LTPAFHYDILKP-YVGLMADSVRVMLDKWEellgqDSPLEVFQ-HVSLMTLDTIMKCAFS 203
Cdd:cd11043   53 SSLLTVSG---EEHKRLrglLLSFLGPEALKDrLLGDIDELVRQHLDSWW-----RGKSVVVLeLAKKMTFELICKLLLG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 204 HQGSIQVDRNSQSYIQAISDLN----NLVFSRVRNAFHqndtiysltsagrwthrACQLAHQHTDQVIQLRKAQLQKEGE 279
Cdd:cd11043  125 IDPEEVVEELRKEFQAFLEGLLsfplNLPGTTFHRALK-----------------ARKRIRKELKKIIEERRAELEKASP 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 280 LEkikrkrhlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE---IHSLLG 356
Cdd:cd11043  188 KG--------DLLDVLLEEKDEDGDSLTDEEILDNILTLLFAGHETTSTTLTLAVKFLAENPKVLQELLEEheeIAKRKE 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 357 DGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 436
Cdd:cd11043  260 EGEGLTWEDYKSMKYTWQVINETLRLAPIVPGVFRKALQDVEY-KGYTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW 338
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158937242 437 APGSAQHSHAFLPFSGGSRNCIGKQFAmnelKVATALTL------LRFELLPDPTRIPIPIARLvlksKNGIHLRLRR 508
Cdd:cd11043  339 EGKGKGVPYTFLPFGGGPRLCPGAELA----KLEILVFLhhlvtrFRWEVVPDEKISRFPLPRP----PKGLPIRLSP 408
CYP72 cd20642
cytochrome P450 family 72; Cytochrome P450 family 72 (CYP72) belongs to the plant CYP72 clan, ...
75-504 1.25e-50

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: 179.01  E-value: 1.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  75 IQKWVETFPSACPHWLwGGKVRVQLYDPDYMKVILGRSD--PKSHgsYRFLAPWIGYGLLLLNGQTWFQHRRMLTPAFHY 152
Cdd:cd20642    4 IHHTVKTYGKNSFTWF-GPIPRVIIMDPELIKEVLNKVYdfQKPK--TNPLTKLLATGLASYEGDKWAKHRKIINPAFHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 153 DILKPYVGLMADSVRVMLDKWEELLGQD--SPLEVFQHVSLMTLDTIMKCAFshqGSiqvdrnsqSYIQAISdlnnlVFS 230
Cdd:cd20642   81 EKLKNMLPAFYLSCSEMISKWEKLVSSKgsCELDVWPELQNLTSDVISRTAF---GS--------SYEEGKK-----IFE 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 231 RVRN-AFHQNDTIYSLTSAGRW-----THRacqlahqhtdqviQLRKAQLQKEGELEKIKRKR----------HLDFLDI 294
Cdd:cd20642  145 LQKEqGELIIQALRKVYIPGWRflptkRNR-------------RMKEIEKEIRSSLRGIINKRekamkageatNDDLLGI 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 295 LLLA------KMENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASiTWNHLD 367
Cdd:cd20642  212 LLESnhkeikEQGNKNGgMSTEDVIEECKLFYFAGQETTSVLLVWTMVLLSQHPDWQERAREEVLQVFGNNKP-DFEGLN 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 368 QMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWPN-PEVFDPFRFAPGSAQHSH- 445
Cdd:cd20642  291 HLKVVTMILYEVLRLYPPVIQLTRAIHKDTKLGD-LTLPAGVQVSLPILLVHRDPELWGDdAKEFNPERFAEGISKATKg 369
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158937242 446 --AFLPFSGGSRNCIGKQFAMNELKVATALTLLRF--ELLPDPTRIPIPIarLVLKSKNGIHL 504
Cdd:cd20642  370 qvSYFPFGWGPRICIGQNFALLEAKMALALILQRFsfELSPSYVHAPYTV--LTLQPQFGAHL 430
PLN02290 PLN02290
cytokinin trans-hydroxylase
110-509 1.00e-45

cytokinin trans-hydroxylase


Pssm-ID: 215164 [Multi-domain]  Cd Length: 516  Bit Score: 167.68  E-value: 1.00e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 110 GRSDPKSHGSYRFlapwIGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQ-DSPLEVFQH 188
Cdd:PLN02290 127 GKSWLQQQGTKHF----IGRGLLMANGADWYHQRHIAAPAFMGDRLKGYAGHMVECTKQMLQSLQKAVESgQTEVEIGEY 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 189 VSLMTLDTIMKCAFSHQgsiqVDRNSQSYiQAISDLNNLVFSRVRNAF---------HQNDTIYSLTSagrwthracqla 259
Cdd:PLN02290 203 MTRLTADIISRTEFDSS----YEKGKQIF-HLLTVLQRLCAQATRHLCfpgsrffpsKYNREIKSLKG------------ 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 260 hqhtdQVIQLRKAQLQKEGELEKIKRKR-HLDFLDILLLAKME----NGSILSDKDLRAEVDTFMFEGHDTTASGISWIL 334
Cdd:PLN02290 266 -----EVERLLMEIIQSRRDCVEIGRSSsYGDDLLGMLLNEMEkkrsNGFNLNLQLIMDECKTFFFAGHETTALLLTWTL 340
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 335 YALATHPKHQERCREEIHSLLGdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLS 414
Cdd:PLN02290 341 MLLASNPTWQDKVRAEVAEVCG-GETPSVDHLSKLTLLNMVINESLRLYPPATLLPRMAFEDIKLGDLH-IPKGLSIWIP 418
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 415 IYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIAR 493
Cdd:PLN02290 419 VLAIHHSEELWgKDANEFNPDRFAGRPFAPGRHFIPFAAGPRNCIGQAFAMMEAKIILAMLISKFSFTISDNYRHAPVVV 498
                        410
                 ....*....|....*.
gi 158937242 494 LVLKSKNGIHLRLRRL 509
Cdd:PLN02290 499 LTIKPKYGVQVCLKPL 514
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
101-480 2.19e-45

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: 164.32  E-value: 2.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 101 DPDYMKVILGrsdpksHGSYRFLAPWigYGLLLLNGQTWF---------QHRRMLTPAFHYDILKPYVGLMADSVRVMLD 171
Cdd:cd11061   15 DPDALKDIYG------HGSNCLKGPF--YDALSPSASLTFttrdkaehaRRRRVWSHAFSDKALRGYEPRILSHVEQLCE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 172 KWEELLGQDS--PLEVFQHVSLMTLDTIMKCAFSHQ-GSIqvDRNSQSYIQAISDLNNLVFSRVRNAfhqnDTIYSLTSA 248
Cdd:cd11061   87 QLDDRAGKPVswPVDMSDWFNYLSFDVMGDLAFGKSfGML--ESGKDRYILDLLEKSMVRLGVLGHA----PWLRPLLLD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 249 GRWTHRAcqlaHQHTDQVIQLRKAQLQKEGELEKIKRKrhlDFLDILLLAKM-ENGSILSDKDLRAEVDTFMFEGHDTTA 327
Cdd:cd11061  161 LPLFPGA----TKARKRFLDFVRAQLKERLKAEEEKRP---DIFSYLLEAKDpETGEGLDLEELVGEARLLIVAGSDTTA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 328 SGISWILYALATHPKHQERCREEIHSLLGDGASI-TWNHLDQMPYTTMCIKEALRLYPPVPGIG-RElsTP---VTFpDG 402
Cdd:cd11061  234 TALSAIFYYLARNPEAYEKLRAELDSTFPSDDEIrLGPKLKSLPYLRACIDEALRLSPPVPSGLpRE--TPpggLTI-DG 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 403 RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH---AFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd11061  311 EYIPGGTTVSVPIYSIHRDERYFPDPFEFIPERWLSRPEELVRarsAFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYD 390

                 .
gi 158937242 480 L 480
Cdd:cd11061  391 F 391
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
281-505 1.54e-43

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: 159.50  E-value: 1.54e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 281 EKIKRKRHLDFLDILLLAKMENGS----ILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG 356
Cdd:cd20650  195 LDSTQKHRVDFLQLMIDSQNSKETeshkALSDLEILAQSIIFIFAGYETTSSTLSFLLYELATHPDVQQKLQEEIDAVLP 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 357 DGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF 436
Cdd:cd20650  275 NKAPPTYDTVMQMEYLDMVVNETLRLFPIAGRLERVCKKDVEI-NGVFIPKGTVVMIPTYALHRDPQYWPEPEEFRPERF 353
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158937242 437 APGSAQH--SHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLP-DPTRIPIPIARL-VLKSKNGIHLR 505
Cdd:cd20650  354 SKKNKDNidPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNFSFKPcKETQIPLKLSLQgLLQPEKPIVLK 426
CYP57A1-like cd11060
cytochrome P450 family 57, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
101-486 2.04e-42

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: 156.59  E-value: 2.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 101 DPDYMKVILGRSDPKS-HGSYRFLAPWIGYGLLLL---NGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEEL 176
Cdd:cd11060   15 DPEAIKTIYGTRSPYTkSDWYKAFRPKDPRKDNLFserDEKRHAALRRKVASGYSMSSLLSLEPFVDECIDLLVDLLDEK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 177 LGQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQVDRNSQSYIQAIsDLNNLVFSRV------RNAFHQNDTIYSLTSAG 249
Cdd:cd11060   95 AVSGKEVDLGKWLQYFAFDVIGEITFGKPfGFLEAGTDVDGYIASI-DKLLPYFAVVgqipwlDRLLLKNPLGPKRKDKT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 250 RWTHracqlahqhtdqVIQLRKAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASG 329
Cdd:cd11060  174 GFGP------------LMRFALEAVAERLAEDAESAKGRKDMLDSFLEAGLKDPEKVTDREVVAEALSNILAGSDTTAIA 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 330 ISWILYALATHPKHQERCREEIHSLLGDGAS---ITWNHLDQMPYTTMCIKEALRLYPPVpGIGRELSTP---VTFPdGR 403
Cdd:cd11060  242 LRAILYYLLKNPRVYAKLRAEIDAAVAEGKLsspITFAEAQKLPYLQAVIKEALRLHPPV-GLPLERVVPpggATIC-GR 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 404 SLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF--APGS--AQHSHAFLPFSGGSRNCIGKQFAMNEL-KVATALtLLR 477
Cdd:cd11060  320 FIPGGTIVGVNPWVIHRDKEVFgEDADVFRPERWleADEEqrRMMDRADLTFGAGSRTCLGKNIALLELyKVIPEL-LRR 398
                        410
                 ....*....|
gi 158937242 478 FEL-LPDPTR 486
Cdd:cd11060  399 FDFeLVDPEK 408
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
136-499 1.27e-41

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: 154.29  E-value: 1.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 136 GQTWFQHRRMLTPAFHY--DILKPYVGLMADSVRVMLDKWEELLGQdsPLEVFQHVSLMTLDTImkCAFSHQGSIQVDRN 213
Cdd:cd11027   59 SPTWKLHRKLAHSALRLyaSGGPRLEEKIAEEAEKLLKRLASQEGQ--PFDPKDELFLAVLNVI--CSITFGKRYKLDDP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 214 SqsyIQAISDLNNlVFSRVRNAFHQNDTIYSLtsagRW----THRACQLAHQHTDQVIQlRKAQLQKEGELEKIKRkrhl 289
Cdd:cd11027  135 E---FLRLLDLND-KFFELLGAGSLLDIFPFL----KYfpnkALRELKELMKERDEILR-KKLEEHKETFDPGNIR---- 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLAKME-------NGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT 362
Cdd:cd11027  202 DLTDALIKAKKEaedegdeDSGLLTDDHLVMTISDIFGAGTETTATTLRWAIAYLVNYPEVQAKLHAELDDVIGRDRLPT 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 363 WNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 441
Cdd:cd11027  282 LSDRKRLPYLEATIAEVLRLSSVVPlALPHKTTCDTTL-RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFRPERFLDENG 360
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158937242 442 Q---HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPI---PIARLVLKSK 499
Cdd:cd11027  361 KlvpKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEGEPPPeleGIPGLVLYPL 424
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
92-507 8.75e-41

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: 152.09  E-value: 8.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  92 GGKVRVQLYDPDYMKVILgRSDPKShgsYRFLAPWI-------GYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMAD 164
Cdd:cd11083    9 GRQPVLVISDPELIREVL-RRRPDE---FRRISSLEsvfremgINGVFSAEGDAWRRQRRLVMPAFSPKHLRYFFPTLRQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 165 SVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQ-GSIQVDRNsqsyiqAISDLNNLVF----SRVRNAFHQN 239
Cdd:cd11083   85 ITERLRERWERAAAEGEAVDVHKDLMRYTVDVTTSLAFGYDlNTLERGGD------PLQEHLERVFpmlnRRVNAPFPYW 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 240 DtiYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELekikRKRHLDfLDILLLAKMENGSILSDKDLRAEVDTFM 319
Cdd:cd11083  159 R--YLRLPADRALDRALVEVRALVLDIIAAARARLAANPAL----AEAPET-LLAMMLAEDDPDARLTDDEIYANVLTLL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 320 FEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT-WNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVT 398
Cdd:cd11083  232 LAGEDTTANTLAWMLYYLASRPDVQARVREEVDAVLGGARVPPlLEALDRLPYLEAVARETLRLKPVAPLLFLEPNEDTV 311
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 399 FpDGRSLPKG--IMVLLSIYGLhhNPKVWPNPEVFDPFRF-APGSAQHSH---AFLPFSGGSRNCIGKQFAMNELKVATA 472
Cdd:cd11083  312 V-GDIALPAGtpVFLLTRAAGL--DAEHFPDPEEFDPERWlDGARAAEPHdpsSLLPFGAGPRLCPGRSLALMEMKLVFA 388
                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 158937242 473 LTLLRFEL-LPDPTRIPIPIARLVLKSKNgihLRLR 507
Cdd:cd11083  389 MLCRNFDIeLPEPAPAVGEEFAFTMSPEG---LRVR 421
PTZ00404 PTZ00404
cytochrome P450; Provisional
97-480 1.71e-40

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 152.57  E-value: 1.71e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  97 VQLYDPDYMKVIL------GRSDPKS----HGSYrflapwiGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:PTZ00404  75 VVLSDPILIREMFvdnfdnFSDRPKIpsikHGTF-------YHGIVTSSGEYWKRNREIVGKAMRKTNLKHIYDLLDDQV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 167 RVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNS---QSYIQAISDL-NNLVFSRVRNAFHQNDTI 242
Cdd:PTZ00404 148 DVLIESMKKIESSGETFEPRYYLTKFTMSAMFKYIFNEDISFDEDIHNgklAELMGPMEQVfKDLGSGSLFDVIEITQPL 227
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 243 YSLtsagrWThracqlahQHTDQVI-QLRKAQLQKEGE-LEKIKRKRHLDFLDILLlakMENGSILSDKDLR--AEVDTF 318
Cdd:PTZ00404 228 YYQ-----YL--------EHTDKNFkKIKKFIKEKYHEhLKTIDPEVPRDLLDLLI---KEYGTNTDDDILSilATILDF 291
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 319 MFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPV 397
Cdd:PTZ00404 292 FLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRNKVLLSDRQSTPYTVAIIKETLRYKPVSPfGLPRSTSNDI 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 398 TFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAqhSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLR 477
Cdd:PTZ00404 372 IIGGGHFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPDS--NDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILN 449

                 ...
gi 158937242 478 FEL 480
Cdd:PTZ00404 450 FKL 452
PLN02738 PLN02738
carotene beta-ring hydroxylase
91-512 4.47e-40

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 153.53  E-value: 4.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  91 WGGKVRVQLYDPDYMKVILgRSDPKSHgSYRFLAPWI----GYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSV 166
Cdd:PLN02738 172 FGPKSFLIVSDPSIAKHIL-RDNSKAY-SKGILAEILefvmGKGLIPADGEIWRVRRRAIVPALHQKYVAAMISLFGQAS 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 167 RVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHqgsiqvDRNSQSYIQAISDLnnlVFSRVRNAFHQNDTIY--- 243
Cdd:PLN02738 250 DRLCQKLDAAASDGEDVEMESLFSRLTLDIIGKAVFNY------DFDSLSNDTGIVEA---VYTVLREAEDRSVSPIpvw 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 244 ------SLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEgEL---EKIKRKRHLDFLDILLLAkmenGSILSDKDLRAE 314
Cdd:PLN02738 321 eipiwkDISPRQRKVAEALKLINDTLDDLIAICKRMVEEE-ELqfhEEYMNERDPSILHFLLAS----GDDVSSKQLRDD 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 315 VDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASiTWNHLDQMPYTTMCIKEALRLYPPVPG-IGREL 393
Cdd:PLN02738 396 LMTMLIAGHETSAAVLTWTFYLLSKEPSVVAKLQEEVDSVLGDRFP-TIEDMKKLKYTTRVINESLRLYPQPPVlIRRSL 474
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 394 STPV--TFPDGRslpkGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-----PGSAQHSHAFLPFSGGSRNCIGKQFAMNE 466
Cdd:PLN02738 475 ENDMlgGYPIKR----GEDIFISVWNLHRSPKHWDDAEKFNPERWPldgpnPNETNQNFSYLPFGGGPRKCVGDMFASFE 550
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 158937242 467 LKVATALTLLRFELLPDPTRIPIPIAR-LVLKSKNGIHLRLRRLPNP 512
Cdd:PLN02738 551 NVVATAMLVRRFDFQLAPGAPPVKMTTgATIHTTEGLKMTVTRRTKP 597
CYP60B-like cd11058
cytochrome P450 family 60, subfamily B and similar cytochrome P450s; This family is composed ...
142-487 6.61e-40

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: 149.27  E-value: 6.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 142 HRRMLTPAF-------HYDILKPYVGLMadsvrvmLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSH-QGSIQvDRN 213
Cdd:cd11058   61 LRRLLAHAFsekalreQEPIIQRYVDLL-------VSRLRERAGSGTPVDMVKWFNFTTFDIIGDLAFGEsFGCLE-NGE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 214 SQSYIQAIsdLNNLVFSRVRNAFHQNDTIYSLTsagRWTHRAcqlahqhtdQVIQLRKAQLQKEGEleKIKRKRHL---- 289
Cdd:cd11058  133 YHPWVALI--FDSIKALTIIQALRRYPWLLRLL---RLLIPK---------SLRKKRKEHFQYTRE--KVDRRLAKgtdr 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 -DFLDiLLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQ 368
Cdd:cd11058  197 pDFMS-YILRNKDEKKGLTREELEANASLLIIAGSETTATALSGLTYYLLKNPEVLRKLVDEIRSAFSSEDDITLDSLAQ 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 369 MPYTTMCIKEALRLYPPVP-GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ----- 442
Cdd:cd11058  276 LPYLNAVIQEALRLYPPVPaGLPRVVPAGGATIDGQFVPGGTSVSVSQWAAYRSPRNFHDPDEFIPERWLGDPRFefdnd 355
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 158937242 443 HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRI 487
Cdd:cd11058  356 KKEAFQPFSVGPRNCIGKNLAYAEMRLILAKLLWNFDLELDPESE 400
PLN02936 PLN02936
epsilon-ring hydroxylase
128-483 1.92e-39

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 149.56  E-value: 1.92e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 128 GYGLLLLNGQTWFQHRRMLTPAFHydilKPYVGLMADSV-----RVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAF 202
Cdd:PLN02936  96 GSGFAIAEGELWTARRRAVVPSLH----RRYLSVMVDRVfckcaERLVEKLEPVALSGEAVNMEAKFSQLTLDVIGLSVF 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 203 SHQ-GSIQVDrnsQSYIQAISDLNNLVFSRVRN--AFHQNDTIYSLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGE 279
Cdd:PLN02936 172 NYNfDSLTTD---SPVIQAVYTALKEAETRSTDllPYWKVDFLCKISPRQIKAEKAVTVIRETVEDLVDKCKEIVEAEGE 248
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 280 leKIKRKRHLDFLD--IL--LLAKMENgsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLL 355
Cdd:PLN02936 249 --VIEGEEYVNDSDpsVLrfLLASREE---VSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVL 323
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 356 GdGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 435
Cdd:PLN02936 324 Q-GRPPTYEDIKELKYLTRCINESMRLYPHPPVLIRRAQVEDVLPGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPER 402
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158937242 436 F-----APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLR--FELLPD 483
Cdd:PLN02936 403 FdldgpVPNETNTDFRYIPFSGGPRKCVGDQFALLEAIVALAVLLQRldLELVPD 457
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
131-491 2.87e-39

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: 147.72  E-value: 2.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 131 LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLdkwEELLgqDSPLEVFQHVSLMTLDTIMKCAFshqGsIQV 210
Cdd:cd11065   54 LLMPYGPRWRLHRRLFHQLLNPSAVRKYRPLQELESKQLL---RDLL--ESPDDFLDHIRRYAASIILRLAY---G-YRV 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 211 DRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTS------------AGRWTHRACQLAHQHTDQViqlrkaqlqkeg 278
Cdd:cd11065  125 PSYDDPLLRDAEEAMEGFSEAGSPGAYLVDFFPFLRYlpswlgapwkrkARELRELTRRLYEGPFEAA------------ 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 279 eLEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG 358
Cdd:cd11065  193 -KERMASGTATPSFVKDLLEELDKEGGLSEEEIKYLAGSLYEAGSDTTASTLQTFILAMALHPEVQKKAQEELDRVVGPD 271
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 359 ASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF- 436
Cdd:cd11065  272 RLPTFEDRPNLPYVNAIVKEVLRWRPVAPlGIPHALTEDDEY-EGYFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYl 350
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 437 ---APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLP--DPTRIPIPI 491
Cdd:cd11065  351 ddpKGTPDPPDPPHFAFGFGRRICPGRHLAENSLFIAIARLLWAFDIKKpkDEGGKEIPD 410
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
141-471 1.92e-34

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: 134.56  E-value: 1.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 141 QHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeelLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYIQA 220
Cdd:cd20638   81 HRKKVIMRAFSREALENYVPVIQEEVRSSVNQW---LQSGPCVLVYPEVKRLMFRIAMRILLGFEPQQTDREQEQQLVEA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 221 ISDLnnlvfsrVRNAFHQN-DTIYSLTSAGRwthRACQLAHQHTDQVIqlrKAQLQKEGELEKIKrkrhlDFLDILLLAK 299
Cdd:cd20638  158 FEEM-------IRNLFSLPiDVPFSGLYRGL---RARNLIHAKIEENI---RAKIQREDTEQQCK-----DALQLLIEHS 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 300 MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHS--LLG----DGASITWNHLDQMPYTT 373
Cdd:cd20638  220 RRNGEPLNLQALKESATELLFGGHETTASAATSLIMFLGLHPEVLQKVRKELQEkgLLStkpnENKELSMEVLEQLKYTG 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 374 MCIKEALRLYPPVPGIGR-ELSTPVTfpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH--AFLPF 450
Cdd:cd20638  300 CVIKETLRLSPPVPGGFRvALKTFEL--NGYQIPKGWNVIYSICDTHDVADIFPNKDEFNPDRFMSPLPEDSSrfSFIPF 377
                        330       340
                 ....*....|....*....|.
gi 158937242 451 SGGSRNCIGKQFAMNELKVAT 471
Cdd:cd20638  378 GGGSRSCVGKEFAKVLLKIFT 398
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
257-485 1.34e-33

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: 131.99  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 257 QLAHQHTDQVIQlrkaqlQKEGELEKIKRKRHLDFLDILLLAKMEngsiLSDKDLRAEVDTFMFEGHDTTASGISWILYA 336
Cdd:cd11062  181 ESIAKQVDEVLR------QVSAGDPPSIVTSLFHALLNSDLPPSE----KTLERLADEAQTLIGAGTETTARTLSVATFH 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 337 LATHPKHQERCREEIHSLLGDGASI-TWNHLDQMPYTTMCIKEALRLYPPVPG-----IGRElstPVTFpDGRSLPKGIM 410
Cdd:cd11062  251 LLSNPEILERLREELKTAMPDPDSPpSLAELEKLPYLTAVIKEGLRLSYGVPTrlprvVPDE---GLYY-KGWVIPPGTP 326
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158937242 411 VLLSIYGLHHNPKVWPNPEVFDPFR-FAPGSAQHSHAFL-PFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPT 485
Cdd:cd11062  327 VSMSSYFVHHDEEIFPDPHEFRPERwLGAAEKGKLDRYLvPFSKGSRSCLGINLAYAELYLALAALFRRFDLELYET 403
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
267-484 1.87e-33

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: 131.60  E-value: 1.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 267 IQLRKAQLQKEGElekikRKRHLDFL--DILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 344
Cdd:cd11075  191 IRARRKRRASGEA-----DKDYTDFLllDLLDLKEEGGERKLTDEELVSLCSEFLNAGTDTTATALEWAMAELVKNPEIQ 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 345 ERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPK 423
Cdd:cd11075  266 EKLYEEIKEVVGDEAVVTEEDLPKMPYLKAVVLETLRRHPPGHfLLPHAVTEDTVL-GGYDIPAGAEVNFNVAAIGRDPK 344
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 424 VWPNPEVFDPFRF---------APGSAQHShaFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDP 484
Cdd:cd11075  345 VWEDPEEFKPERFlaggeaadiDTGSKEIK--MMPFGAGRRICPGLGLATLHLELFVARLVQEFEWKLVE 412
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
131-503 4.37e-33

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: 131.11  E-value: 4.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 131 LLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFSHQGSIQV 210
Cdd:cd20649   52 LLCLRDERWKRVRSILTPAFSAAKMKEMVPLINQACDVLLRNLKSYAESGNAFNIQRCYGCFTMDVVASVAFGTQVDSQK 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 211 DRN-----------SQSYIQAI-----------------------SDLNNLVFSRVRNAFHQNDtiySLTSAGR------ 250
Cdd:cd20649  132 NPDdpfvknckrffEFSFFRPIlilflafpfimiplarilpnksrDELNSFFTQCIRNMIAFRD---QQSPEERrrdflq 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 251 WT----HRACQLAHQHTDQVIQLRKAQLQK---EGELEKIKRKRhldfldillLAKMengsiLSDKDLRAEVDTFMFEGH 323
Cdd:cd20649  209 LMldarTSAKFLSVEHFDIVNDADESAYDGhpnSPANEQTKPSK---------QKRM-----LTEDEIVGQAFIFLIAGY 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGR 403
Cdd:cd20649  275 ETTTNTLSFATYLLATHPECQKKLLREVDEFFSKHEMVDYANVQELPYLDMVIAETLRMYPPAFRFAREAAEDCVV-LGQ 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 404 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSH--AFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELL 481
Cdd:cd20649  354 RIPAGAVLEIPVGFLHHDPEHWPEPEKFIPERFTAEAKQRRHpfVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQ 433
                        410       420
                 ....*....|....*....|....
gi 158937242 482 PDP-TRIPIPI-ARLVLKSKNGIH 503
Cdd:cd20649  434 ACPeTEIPLQLkSKSTLGPKNGVY 457
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
245-508 6.74e-32

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: 127.41  E-value: 6.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 245 LTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEgelekiKRKRHLDFLDILllakMENGSILSDKDLRAEVDTFM---FE 321
Cdd:cd11041  169 FLPEPRRLRRLLRRARPLIIPEIERRRKLKKGP------KEDKPNDLLQWL----IEAAKGEGERTPYDLADRQLalsFA 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 322 GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFP 400
Cdd:cd11041  239 AIHTTSMTLTHVLLDLAAHPEYIEPLREEIRSVLAEHGGWTKAALNKLKKLDSFMKESQRLNPLSLvSLRRKVLKDVTLS 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 401 DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-----PGSAQHSHA------FLPFSGGSRNCIGKQFAMNELKV 469
Cdd:cd11041  319 DGLTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFYrlreqPGQEKKHQFvstspdFLGFGHGRHACPGRFFASNEIKL 398
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 158937242 470 ATALTLLRFEL-----LPDPTRIPIPIARLVLkSKNGIHLRLRR 508
Cdd:cd11041  399 ILAHLLLNYDFklpegGERPKNIWFGEFIMPD-PNAKVLVRRRE 441
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
111-504 1.11e-31

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: 126.79  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 111 RSDPKSHGSYRFLAPwIGYGLLLLNGQTWFQHRRMLTPAfhydILKP-----YVGLMADSVRVMLDKWEELLGQDSP--- 182
Cdd:cd20648   40 RSDLSSWKDYRQLRG-HAYGLLTAEGEEWQRLRSLLAKH----MLKPkaveaYAGVLNAVVTDLIRRLRRQRSRSSPgvv 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 183 LEVFQHVSLMTLDTIMKCAF-SHQGSI--QVDRNSQSYIQAIsdlnNLVFsrvrnafhqndTIYSLTSA-GRWTHRA--- 255
Cdd:cd20648  115 KDIAGEFYKFGLEGISSVLFeSRIGCLeaNVPEETETFIQSI----NTMF-----------VMTLLTMAmPKWLHRLfpk 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 256 -----CQ-------LAHQHTDQVIQLRKAQLQKEGELEKikrkRHLDFLdillLAKMEngsiLSDKDLRAEVDTFMFEGH 323
Cdd:cd20648  180 pwqrfCRswdqmfaFAKGHIDRRMAEVAAKLPRGEAIEG----KYLTYF----LAREK----LPMKSIYGNVTELLLAGV 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR 403
Cdd:cd20648  248 DTISSTLSWSLYELSRHPDVQTALHREITAALKDNSVPSAADVARMPLLKAVVKEVLRLYPVIPGNARVIPDRDIQVGEY 327
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 404 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLP 482
Cdd:cd20648  328 IIPKKTLITLCHYATSRDENQFPDPNSFRPERWlGKGDTHHPYASLPFGFGKRSCIGRRIAELEVYLALARILTHFEVRP 407
                        410       420
                 ....*....|....*....|...
gi 158937242 483 DPTRIPI-PIARLVLKSKNGIHL 504
Cdd:cd20648  408 EPGGSPVkPMTRTLLVPERSINL 430
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
280-488 2.48e-31

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: 125.41  E-value: 2.48e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 280 LEKIKRKRHLDFLDiLLLAKMENG----SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLL 355
Cdd:cd20651  192 KKTYDEDNPRDLID-AYLREMKKKeppsSSFTDDQLVMICLDLFIAGSETTSNTLGFAFLYLLLNPEVQRKVQEEIDEVV 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 356 GDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 435
Cdd:cd20651  271 GRDRLPTLDDRSKLPYTEAVILEVLRIFTLVPIGIPHRALKDTTLGGYRIPKDTTILASLYSVHMDPEYWGDPEEFRPER 350
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158937242 436 F--APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIP 488
Cdd:cd20651  351 FldEDGKLLKDEWFLPFGAGKRRCLGESLARNELFLFFTGLLQNFTFSPPNGSLP 405
CYP71-like cd11072
cytochrome P450 family 71 and similar cytochrome P450s; The group includes plant cytochrome ...
166-487 6.77e-31

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: 124.50  E-value: 6.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 166 VRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFshqGSIQVDRNSQSYIQAISDLNNLV--F-------------- 229
Cdd:cd11072   91 VSLLVKKIRESASSSSPVNLSELLFSLTNDIVCRAAF---GRKYEGKDQDKFKELVKEALELLggFsvgdyfpslgwidl 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 230 -----SRVRNAFHQNDTIYsltsagrwthracqlahqhtDQVIQLRKAQLQKEGELEkikrkrHLDFLDILLLAKMENGS 304
Cdd:cd11072  168 ltgldRKLEKVFKELDAFL--------------------EKIIDEHLDKKRSKDEDD------DDDDLLDLRLQKEGDLE 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 305 I-LSDKDLRAEV-DtfMFE-GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALR 381
Cdd:cd11072  222 FpLTRDNIKAIIlD--MFLaGTDTSATTLEWAMTELIRNPRVMKKAQEEVREVVGGKGKVTEEDLEKLKYLKAVIKETLR 299
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 382 LYPPVPGIG-RELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA---QHSHAFLPFSGGSRNC 457
Cdd:cd11072  300 LHPPAPLLLpRECREDCKI-NGYDIPAKTRVIVNAWAIGRDPKYWEDPEEFRPERFLDSSIdfkGQDFELIPFGAGRRIC 378
                        330       340       350
                 ....*....|....*....|....*....|.
gi 158937242 458 IGKQFAMNELKVATALTLLRFEL-LPDPTRI 487
Cdd:cd11072  379 PGITFGLANVELALANLLYHFDWkLPDGMKP 409
CYP61_CYP710 cd11082
C-22 sterol desaturase subfamily, such as fungal cytochrome P450 61 and plant cytochrome P450 ...
307-479 1.47e-30

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: 123.13  E-value: 1.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 307 SDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPP 385
Cdd:cd11082  217 SDEEIAGTLLDFLFASQDASTSSLVWALQLLADHPDVLAKVREEQARLRPNDePPLTLDLLEEMKYTRQVVKEVLRYRPP 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 386 VPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPkvWPNPEVFDPFRFAPGSA---QHSHAFLPFSGGSRNCIGKQF 462
Cdd:cd11082  297 APMVPHIAKKDFPLTEDYTVPKGTIVIPSIYDSCFQG--FPEPDKFDPDRFSPERQedrKYKKNFLVFGAGPHQCVGQEY 374
                        170
                 ....*....|....*....
gi 158937242 463 AMNELKVATAL--TLLRFE 479
Cdd:cd11082  375 AINHLMLFLALfsTLVDWK 393
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
135-500 2.45e-30

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: 122.79  E-value: 2.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 135 NGQTWFQHRRMLTPAFHYDILKPYVGLMADSV----RVMLDKWEELLGQDSPL----EVFQHVSlmtlDTIMKCAFSHQg 206
Cdd:cd11028   57 YGPRWKLHRKLAQNALRTFSNARTHNPLEEHVteeaEELVTELTENNGKPGPFdprnEIYLSVG----NVICAICFGKR- 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 207 siqVDRNSQSYIQAISdlNNLVFSRVRNAFHQNDTIYSLtsagRWthracqLAHQHTDQVIQLRKAqlqkegeLEKI--- 283
Cdd:cd11028  132 ---YSRDDPEFLELVK--SNDDFGAFVGAGNPVDVMPWL----RY------LTRRKLQKFKELLNR-------LNSFilk 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 284 KRKRHL---------DFLDILLLAKMEN------GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 348
Cdd:cd11028  190 KVKEHLdtydkghirDITDALIKASEEKpeeekpEVGLTDEHIISTVQDLFGAGFDTISTTLQWSLLYMIRYPEIQEKVQ 269
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 349 EEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPgigrelstpVTFP---------DGRSLPKGIMVLLSIYGLH 419
Cdd:cd11028  270 AELDRVIGRERLPRLSDRPNLPYTEAFILETMRHSSFVP---------FTIPhattrdttlNGYFIPKGTVVFVNLWSVN 340
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 420 HNPKVWPNPEVFDPFRFAPGSAQ----HSHAFLPFSGGSRNCIGKQFAMNE--LKVATALTLLRFELLPDPTRIPIPIAR 493
Cdd:cd11028  341 HDEKLWPDPSVFRPERFLDDNGLldktKVDKFLPFGAGRRRCLGEELARMElfLFFATLLQQCEFSVKPGEKLDLTPIYG 420

                 ....*..
gi 158937242 494 LVLKSKN 500
Cdd:cd11028  421 LTMKPKP 427
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
322-488 4.50e-30

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: 122.13  E-value: 4.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 322 GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFp 400
Cdd:cd20652  246 GVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPDLVTLEDLSSLPYLQACISESQRIRSVVPlGIPHGCTEDAVL- 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 401 DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRF 478
Cdd:cd20652  325 AGYRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFldTDGKYLKPEAFIPFQTGKRMCLGDELARMILFLFTARILRKF 404
                        170
                 ....*....|.
gi 158937242 479 EL-LPDPTRIP 488
Cdd:cd20652  405 RIaLPDGQPVD 415
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
166-485 4.82e-30

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: 121.89  E-value: 4.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 166 VRVMLDKWEELLGQDSPLEVFQHVSLMTLDTIMKCAFS---HQGSIQVDRNSQSYIQAISDLNNLVfsrvrNAFHQNDTI 242
Cdd:cd20618   89 LSHLVKSLLEESESGKPVNLREHLSDLTLNNITRMLFGkryFGESEKESEEAREFKELIDEAFELA-----GAFNIGDYI 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 243 YSLtsagRW-----THRACQLAHQHTDQVIQlrkAQLQKEGELEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDT 317
Cdd:cd20618  164 PWL----RWldlqgYEKRMKKLHAKLDRFLQ---KIIEEHREKRGESKKGGDDDDDLLLLLDLDGEGKLSDDNIKALLLD 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 318 FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTP 396
Cdd:cd20618  237 MLAAGTDTSAVTIEWAMAELLRHPEVMRKAQEELDSVVGRERLVEESDLPKLPYLQAVVKETLRLHPPGPlLLPHESTED 316
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 397 VTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSHaFLPFSGGSRNCIGKQFAMNELKVAT 471
Cdd:cd20618  317 CKV-AGYDIPAGTRVLVNVWAIGRDPKVWEDPLEFKPERFLESDIddvkgQDFE-LLPFGSGRRMCPGMPLGLRMVQLTL 394
                        330
                 ....*....|....*.
gi 158937242 472 AlTLL-RFEL-LPDPT 485
Cdd:cd20618  395 A-NLLhGFDWsLPGPK 409
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
313-485 8.30e-30

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: 121.37  E-value: 8.30e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 313 AEVDTFMfEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRE 392
Cdd:cd20674  230 AVVDLFI-GGTETTASTLSWAVAFLLHHPEIQDRLQEELDRVLGPGASPSYKDRARLPLLNATIAEVLRLRPVVPLALPH 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 393 LSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA-PGSAqhSHAFLPFSGGSRNCIGKQFAMNELKVAT 471
Cdd:cd20674  309 RTTRDSSIAGYDIPKGTVVIPNLQGAHLDETVWEQPHEFRPERFLePGAA--NRALLPFGCGARVCLGEPLARLELFVFL 386
                        170
                 ....*....|....
gi 158937242 472 ALTLLRFELLPDPT 485
Cdd:cd20674  387 ARLLQAFTLLPPSD 400
PLN02655 PLN02655
ent-kaurene oxidase
269-479 1.31e-29

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 121.39  E-value: 1.31e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 269 LRKAQLQKEGELEKikRKRHLDFLdilllakMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 348
Cdd:PLN02655 230 LIKQQKKRIARGEE--RDCYLDFL-------LSEATHLTDEQLMMLVWEPIIEAADTTLVTTEWAMYELAKNPDKQERLY 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 349 EEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNP 428
Cdd:PLN02655 301 REIREVCGDER-VTEEDLPNLPYLNAVFHETLRKYSPVPLLPPRFVHEDTTLGGYDIPAGTQIAINIYGCNMDKKRWENP 379
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158937242 429 EVFDPFRFAPGSAQHS--HAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:PLN02655 380 EEWDPERFLGEKYESAdmYKTMAFGAGKRVCAGSLQAMLIACMAIARLVQEFE 432
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
111-504 1.34e-29

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: 120.54  E-value: 1.34e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 111 RSDPKSHGSYRFLAPWiGYGLLLLNGQTWFQHRRMLTPAfhydILKP-----YVGLMADSVRVMLDKWEELlGQDSPLEV 185
Cdd:cd20646   39 RSDMPHWKEHRDLRGH-AYGPFTEEGEKWYRLRSVLNQR----MLKPkevslYADAINEVVSDLMKRIEYL-RERSGSGV 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 186 FqhVSLMTlDTIMKCAFSHQGSI-----------QVDRNSQSYIQAISDL--NNLVFSRVRNA------FHQN-----DT 241
Cdd:cd20646  113 M--VSDLA-NELYKFAFEGISSIlfetrigclekEIPEETQKFIDSIGEMfkLSEIVTLLPKWtrpylpFWKRyvdawDT 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 242 IYSLtsagrwthracqlAHQHTDQVIQLRKAQLQKEGELEKikrkrhlDFLDILLlakmENGSiLSDKDLRAEVDTFMFE 321
Cdd:cd20646  190 IFSF-------------GKKLIDKKMEEIEERVDRGEPVEG-------EYLTYLL----SSGK-LSPKEVYGSLTELLLA 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 322 GHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPD 401
Cdd:cd20646  245 GVDTTSNTLSWALYHLARDPEIQERLYQEVISVCPGDRIPTAEDIAKMPLLKAVIKETLRLYPVVPGNARVIVEKEVVVG 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 402 GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd20646  325 DYLFPKNTLFHLCHYAVSHDETNFPEPERFKPERWlrDGGLKHHPFGSIPFGYGVRACVGRRIAELEMYLALSRLIKRFE 404
                        410       420
                 ....*....|....*....|....*.
gi 158937242 480 LLPDPTRIPI-PIARLVLKSKNGIHL 504
Cdd:cd20646  405 VRPDPSGGEVkAITRTLLVPNKPINL 430
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
290-487 1.66e-29

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: 120.36  E-value: 1.66e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLaKMEN-----GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 364
Cdd:cd11026  202 DFIDCFLL-KMEKekdnpNSEFHEENLVMTVLDLFFAGTETTSTTLRWALLLLMKYPHIQEKVQEEIDRVIGRNRTPSLE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 365 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 441
Cdd:cd11026  281 DRAKMPYTDAVIHEVQRFGDIVPlGVPHAVTRDTKF-RGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFldEQGKF 359
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 158937242 442 QHSHAFLPFSGGSRNCIGKQFAMNE--LKVATALTLLRFELLPDPTRI 487
Cdd:cd11026  360 KKNEAFMPFSAGKRVCLGEGLARMElfLFFTSLLQRFSLSSPVGPKDP 407
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
265-488 1.39e-28

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: 117.81  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 265 QVIQLRKAQLQKEGELEKIKRKRHL--DFLDILLLAKM----------ENGSILSDKDLRAEVDTFMFEGHDTTASGISW 332
Cdd:cd20673  175 QCVKIRDKLLQKKLEEHKEKFSSDSirDLLDALLQAKMnaennnagpdQDSVGLSDDHILMTVGDIFGAGVETTTTVLKW 254
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 333 ILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPgigreLSTP-VTFPD----GRSLPK 407
Cdd:cd20673  255 IIAFLLHNPEVQKKIQEEIDQNIGFSRTPTLSDRNHLPLLEATIREVLRIRPVAP-----LLIPhVALQDssigEFTIPK 329
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 408 GIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQH----SHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL-LP 482
Cdd:cd20673  330 GTRVVINLWALHHDEKEWDQPDQFMPERFLDPTGSQlispSLSYLPFGAGPRVCLGEALARQELFLFMAWLLQRFDLeVP 409

                 ....*.
gi 158937242 483 DPTRIP 488
Cdd:cd20673  410 DGGQLP 415
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
250-459 3.16e-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: 116.86  E-value: 3.16e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 250 RWTHRACQLAHQHTDQVIQLRKAQLQKEGElekikRKRHLDFLDILLLAKMENGSiLSDKDLRAevdtFMFE----GHDT 325
Cdd:cd11073  177 RRMAEHFGKLFDIFDGFIDERLAEREAGGD-----KKKDDDLLLLLDLELDSESE-LTRNHIKA----LLLDlfvaGTDT 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 326 TASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPG-IGRELSTPVTFpDGRS 404
Cdd:cd11073  247 TSSTIEWAMAELLRNPEKMAKARAELDEVIGKDKIVEESDISKLPYLQAVVKETLRLHPPAPLlLPRKAEEDVEV-MGYT 325
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 158937242 405 LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQ---HSHAFLPFSGGSRNCIG 459
Cdd:cd11073  326 IPKGTQVLVNVWAIGRDPSVWEDPLEFKPERFLGSEIDfkgRDFELIPFGSGRRICPG 383
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
141-489 6.12e-28

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: 116.09  E-value: 6.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 141 QHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWeelLGQDSPLEVFQHVSLMTLDTIMKCAFS-HQGSIQVDRNSQSYIQ 219
Cdd:cd20636   82 QRRKVLARVFSRAALESYLPRIQDVVRSEVRGW---CRGPGPVAVYTAAKSLTFRIAVRILLGlRLEEQQFTYLAKTFEQ 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 220 AISDLNNLV----FSRVRNAFHQNDTIysltsagrwthracqlaHQHTDQVIQlrkaqlqkegelEKIKRKR---HLDFL 292
Cdd:cd20636  159 LVENLFSLPldvpFSGLRKGIKARDIL-----------------HEYMEKAIE------------EKLQRQQaaeYCDAL 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 293 DILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSL-LGDG-----ASITWNHL 366
Cdd:cd20636  210 DYMIHSARENGKELTMQELKESAVELIFAAFSTTASASTSLVLLLLQHPSAIEKIRQELVSHgLIDQcqccpGALSLEKL 289
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 367 DQMPYTTMCIKEALRLYPPVPGIGRelSTPVTFP-DGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPG---SAQ 442
Cdd:cd20636  290 SRLRYLDCVVKEVLRLLPPVSGGYR--TALQTFElDGYQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEreeSKS 367
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 158937242 443 HSHAFLPFSGGSRNCIGKQFAMNELK------VATALTLLRFELLPDPTRIPI 489
Cdd:cd20636  368 GRFNYIPFGGGVRSCIGKELAQVILKtlavelVTTARWELATPTFPKMQTVPI 420
PLN03195 PLN03195
fatty acid omega-hydroxylase; Provisional
192-482 1.39e-26

fatty acid omega-hydroxylase; Provisional


Pssm-ID: 215627 [Multi-domain]  Cd Length: 516  Bit Score: 112.95  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 192 MTLDTIMKCAFSHQ-GSIQVDRNSQSYIQAISDLNNLVFSRVRNAFHQNDTIYSLTSAgRWTHRACQLAHQHTDQVIQLR 270
Cdd:PLN03195 177 MTLDSICKVGFGVEiGTLSPSLPENPFAQAFDTANIIVTLRFIDPLWKLKKFLNIGSE-ALLSKSIKVVDDFTYSVIRRR 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 271 KAQLQK-EGELEKIKRkrhlDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCRE 349
Cdd:PLN03195 256 KAEMDEaRKSGKKVKH----DILSRFIELGEDPDSNFTDKSLRDIVLNFVIAGRDTTATTLSWFVYMIMMNPHVAEKLYS 331
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 350 EIHSLLGDGAS--------------------ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGI 409
Cdd:PLN03195 332 ELKALEKERAKeedpedsqsfnqrvtqfaglLTYDSLGKLQYLHAVITETLRLYPAVPQDPKGILEDDVLPDGTKVKAGG 411
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158937242 410 MVLLSIYGLHHNPKVW-PNPEVFDPFR-FAPGSAQHSHA--FLPFSGGSRNCIGKQFAMNELKVATAL--TLLRFELLP 482
Cdd:PLN03195 412 MVTYVPYSMGRMEYNWgPDAASFKPERwIKDGVFQNASPfkFTAFQAGPRICLGKDSAYLQMKMALALlcRFFKFQLVP 490
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
281-484 1.95e-26

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: 111.41  E-value: 1.95e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 281 EKIKRKRHLDFLDILLL-----AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLL 355
Cdd:cd20666  194 ETLDPANPRDFIDMYLLhieeeQKNNAESSFNEDYLFYIIGDLFIAGTDTTTNTLLWCLLYMSLYPEVQEKVQAEIDTVI 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 356 GDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFR 435
Cdd:cd20666  274 GPDRAPSLTDKAQMPFTEATIMEVQRMTVVVPLSIPHMASENTVLQGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSR 353
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158937242 436 FAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDP 484
Cdd:cd20666  354 FLDENGQliKKEAFIPFGIGRRVCMGEQLAKMELFLMFVSLMQSFTFLLPP 404
CYP78 cd11076
cytochrome P450 family 78; Characterized cytochrome P450 family 78 (CYP78 or Cyp78) proteins ...
289-485 2.15e-26

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: 111.27  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 289 LDFLDILLlaKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQ 368
Cdd:cd11076  205 EDDVDVLL--SLQGEEKLSDSDMIAVLWEMIFRGTDTVAILTEWIMARMVLHPDIQSKAQAEIDAAVGGSRRVADSDVAK 282
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 369 MPYTTMCIKEALRLYPPVPGIG-RELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAF 447
Cdd:cd11076  283 LPYLQAVVKETLRLHPPGPLLSwARLAIHDVTVGGHVVPAGTTAMVNMWAITHDPHVWEDPLEFKPERFVAAEGGADVSV 362
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 158937242 448 L-------PFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPT 485
Cdd:cd11076  363 LgsdlrlaPFGAGRRVCPGKALGLATVHLWVAQLLHEFEWLPDDA 407
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
280-480 6.73e-26

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: 109.99  E-value: 6.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 280 LEKI------KRKRHL-----DFLDILL-LAKMENGSI-LSDKDLRA-EVDTFMfEGHDTTASGISWILYALATHPKHQE 345
Cdd:cd20655  185 LERIikeheeKRKKRKeggskDLLDILLdAYEDENAEYkITRNHIKAfILDLFI-AGTDTSAATTEWAMAELINNPEVLE 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 346 RCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVW 425
Cdd:cd20655  264 KAREEIDSVVGKTRLVQESDLPNLPYLQAVVKETLRLHPPGPLLVRESTEGCKI-NGYDIPEKTTLFVNVYAIMRDPNYW 342
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 158937242 426 PNPEVFDPFRFAPGSA---------QHSHaFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL 480
Cdd:cd20655  343 EDPLEFKPERFLASSRsgqeldvrgQHFK-LLPFGSGRRGCPGASLAYQVVGTAIAAMVQCFDW 405
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
277-481 7.91e-26

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: 110.01  E-value: 7.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 277 EGELEKIKRKR--------HLDFLDILLLAKMENGSIL-SDKD--LRAEVDTFMFEGHDTTASGISWILYALATHPKHQE 345
Cdd:cd20654  197 EEWLEEHRQKRsssgksknDEDDDDVMMLSILEDSQISgYDADtvIKATCLELILGGSDTTAVTLTWALSLLLNNPHVLK 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 346 RCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW 425
Cdd:cd20654  277 KAQEELDTHVGKDRWVEESDIKNLVYLQAIVKETLRLYPPGPLLGPREATEDCTVGGYHVPKGTRLLVNVWKIQRDPNVW 356
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158937242 426 PNPEVFDPFRFAPGSAQ-----HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELL 481
Cdd:cd20654  357 SDPLEFKPERFLTTHKDidvrgQNFELIPFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIK 417
CYP24A1 cd20645
cytochrome P450 family 24, subfamily A, polypeptide 1, also called vitamin D(3) 24-hydroxylase; ...
128-473 8.47e-26

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: 109.51  E-value: 8.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 128 GYGLLLLNGQTWFQHRRmltpAFHYDILKPYV---------GLMADsvrvMLDKWEELLGQDSPLE-VFQHVSLMTLDTI 197
Cdd:cd20645   55 AYGLLILEGQEWQRVRS----AFQKKLMKPKEvmkldgkinEVLAD----FMGRIDELCDETGRVEdLYSELNKWSFETI 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 198 MKCAFSHQ-GSIQ--VDRNSQSYIQAI----SDLNNLVFSRVRnaFHQNdtiyslTSAGRWthracqlaHQHT---DQVI 267
Cdd:cd20645  127 CLVLYDKRfGLLQqnVEEEALNFIKAIktmmSTFGKMMVTPVE--LHKR------LNTKVW--------QDHTeawDNIF 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 268 QLRKAQLQKEgeLEKIKRKRHLDFL-DILllakmeNGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQER 346
Cdd:cd20645  191 KTAKHCIDKR--LQRYSQGPANDFLcDIY------HDNELSKKELYAAITELQIGGVETTANSLLWILYNLSRNPQAQQK 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 347 CREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDgRSLPKGIMVLLSIYGLHHNPKVWP 426
Cdd:cd20645  263 LLQEIQSVLPANQTPRAEDLKNMPYLKACLKESMRLTPSVPFTSRTLDKDTVLGD-YLLPKGTVLMINSQALGSSEEYFE 341
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 158937242 427 NPEVFDPFRF-APGSAQHSHAFLPFSGGSRNCIGKQFAmnELKVATAL 473
Cdd:cd20645  342 DGRQFKPERWlQEKHSINPFAHVPFGIGKRMCIGRRLA--ELQLQLAL 387
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
304-489 1.04e-25

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: 109.33  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 304 SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKH--QERCREEIHSLLGDGASITWNHLDQM--PYTTMCIKEA 379
Cdd:cd11066  222 SKLTDAELQSICLTMVSAGLDTVPLNLNHLIGHLSHPPGQeiQEKAYEEILEAYGNDEDAWEDCAAEEkcPYVVALVKET 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 380 LRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSRN 456
Cdd:cd11066  302 LRYFTVLPlGLPRKTTKDIVY-NGAVIPAGTILFMNAWAANHDPEHFGDPDEFIPERWldASGDLIPGPPHFSFGAGSRM 380
                        170       180       190
                 ....*....|....*....|....*....|...
gi 158937242 457 CIGKQFAMNELKVATALTLLRFELLPDPTRIPI 489
Cdd:cd11066  381 CAGSHLANRELYTAICRLILLFRIGPKDEEEPM 413
CYP26B1 cd20637
cytochrome P450 family 26, subfamily B, polypeptide 1; Cytochrome P450 26B1 (CYP26B1) is a ...
269-491 1.05e-25

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: 109.55  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 269 LRKAQLQKegeLEKIKRKRHLDFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCR 348
Cdd:cd20637  188 LEKAIREK---LQGTQGKDYADALDILIESAKEHGKELTMQELKDSTIELIFAAFATTASASTSLIMQLLKHPGVLEKLR 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 349 EEI--HSLLGDG----ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRelSTPVTFP-DGRSLPKGIMVLLSIYGLHHN 421
Cdd:cd20637  265 EELrsNGILHNGclceGTLRLDTISSLKYLDCVIKEVLRLFTPVSGGYR--TALQTFElDGFQIPKGWSVLYSIRDTHDT 342
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158937242 422 PKVWPNPEVFDPFRFAPGSAQHSHA---FLPFSGGSRNCIGKQFAMNELKV-ATALTLL-RFELLPD--PTRIPIPI 491
Cdd:cd20637  343 APVFKDVDAFDPDRFGQERSEDKDGrfhYLPFGGGVRTCLGKQLAKLFLKVlAVELASTsRFELATRtfPRMTTVPV 419
CYP2J cd20662
cytochrome P450 family 2, subfamily J; Members of CYP2J are expressed in multiple tissues in ...
290-504 1.10e-25

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: 109.12  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILL--LAK-MENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHL 366
Cdd:cd20662  202 DFIDAYLkeMAKyPDPTTSFNEENLICSTLDLFFAGTETTSTTLRWALLYMALYPEIQEKVQAEIDRVIGQKRQPSLADR 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 367 DQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHS 444
Cdd:cd20662  282 ESMPYTNAVIHEVQRMGNIIPlNVPREVAVDTKL-AGFHLPKGTMILTNLTALHRDPKEWATPDTFNPGHFlENGQFKKR 360
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 445 HAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIpipiarLVLKSKNGIHL 504
Cdd:cd20662  361 EAFLPFSMGKRACLGEQLARSELFIFFTSLLQKFTFKPPPNEK------LSLKFRMGITL 414
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
285-471 2.03e-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: 108.66  E-value: 2.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 285 RKRHLDFLDILLLAKMEN--GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASIT 362
Cdd:cd20657  201 RKGKPDFLDFVLLENDDNgeGERLTDTNIKALLLNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRRLL 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 363 WNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGsa 441
Cdd:cd20657  281 ESDIPNLPYLQAICKETFRLHPSTPlNLPRIASEACEV-DGYYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPG-- 357
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 158937242 442 qhSHA----------FLPFSGGSRNCIGKQF--AMNELKVAT 471
Cdd:cd20657  358 --RNAkvdvrgndfeLIPFGAGRRICAGTRMgiRMVEYILAT 397
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
274-494 3.42e-25

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: 107.98  E-value: 3.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 274 LQKEGELEKIKRKRHL--DFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 351
Cdd:cd20661  200 IERFSENRKPQSPRHFidAYLDEMDQNKNDPESTFSMENLIFSVGELIIAGTETTTNVLRWAILFMALYPNIQGQVQKEI 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 352 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPvTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV 430
Cdd:cd20661  280 DLVVGPNGMPSFEDKCKMPYTEAVLHEVLRFCNIVPlGIFHATSKD-AVVRGYSIPKGTTVITNLYSVHFDEKYWSDPEV 358
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158937242 431 FDPFRFAPGSAQ--HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPIPIARL 494
Cdd:cd20661  359 FHPERFLDSNGQfaKKEAFVPFSLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHGLIPDLKPKL 424
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
332-483 3.79e-25

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: 107.84  E-value: 3.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 332 WILYALATHPKHQERCREEIHSLLGDGASITWNH-----LDQMPYTTMCIKEALRLYPpVPGIGRELSTPVTFPDGRSLP 406
Cdd:cd11040  245 WLLAHILSDPELLERIREEIEPAVTPDSGTNAILdltdlLTSCPLLDSTYLETLRLHS-SSTSVRLVTEDTVLGGGYLLR 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 407 KGIMVLLSIYGLHHNPKVW-PNPEVFDPFRF-----APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL 480
Cdd:cd11040  324 KGSLVMIPPRLLHMDPEIWgPDPEEFDPERFlkkdgDKKGRGLPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDV 403

                 ...
gi 158937242 481 LPD 483
Cdd:cd11040  404 EPV 406
CYP79 cd20658
cytochrome P450 family 79; Cytochrome P450 family 79 (CYP79) enzymes catalyze the first ...
255-478 1.03e-24

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: 106.68  E-value: 1.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 255 ACQLAHQHTDQVIQLRkAQLQKEGelekiKRKRHLDFLDILLLAKMENGS-ILSDKDLRAEVDTFMFEGHDTTASGISWI 333
Cdd:cd20658  187 AMRIIRKYHDPIIDER-IKQWREG-----KKKEEEDWLDVFITLKDENGNpLLTPDEIKAQIKELMIAAIDNPSNAVEWA 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 334 LYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLL 413
Cdd:cd20658  261 LAEMLNQPEILRKATEELDRVVGKERLVQESDIPNLNYVKACAREAFRLHPVAPFNVPHVAMSDTTVGGYFIPKGSHVLL 340
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 414 SIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSHAFLPFSGGSRNCIGkqfamneLKVATALTLLRF 478
Cdd:cd20658  341 SRYGLGRNPKVWDDPLKFKPERHLNEDSevtltEPDLRFISFSTGRRGCPG-------VKLGTAMTVMLL 403
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
284-469 1.49e-24

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 106.56  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 284 KRKRHLDFLDiLLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGD---GAS 360
Cdd:PLN02196 239 RRQNGSSHND-LLGSFMGDKEGLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIRKDkeeGES 317
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 361 ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApgS 440
Cdd:PLN02196 318 LTWEDTKKMPLTSRVIQETLRVASILSFTFREAVEDVEY-EGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPSRFE--V 394
                        170       180
                 ....*....|....*....|....*....
gi 158937242 441 AQHSHAFLPFSGGSRNCIGKQFAMNELKV 469
Cdd:PLN02196 395 APKPNTFMPFGNGTHSCPGNELAKLEISV 423
PLN02426 PLN02426
cytochrome P450, family 94, subfamily C protein
268-508 2.14e-24

cytochrome P450, family 94, subfamily C protein


Pssm-ID: 215235 [Multi-domain]  Cd Length: 502  Bit Score: 106.31  E-value: 2.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 268 QLRKAqLQKEGEL--EKIKRKRHLDFLDI--LLLAKMenGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKH 343
Cdd:PLN02426 250 KLKEA-IKLVDELaaEVIRQRRKLGFSASkdLLSRFM--ASINDDKYLRDIVVSFLLAGRDTVASALTSFFWLLSKHPEV 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 344 QERCREEIHSLLGDG-ASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNP 422
Cdd:PLN02426 327 ASAIREEADRVMGPNqEAASFEEMKEMHYLHAALYESMRLFPPVQFDSKFAAEDDVLPDGTFVAKGTRVTYHPYAMGRME 406
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 423 KVW-PNPEVFDPFRFAPGSaqhshAFLP--------FSGGSRNCIGKQFAMNELKvATALTLLR---FELLPDPTRIPIP 490
Cdd:PLN02426 407 RIWgPDCLEFKPERWLKNG-----VFVPenpfkypvFQAGLRVCLGKEMALMEMK-SVAVAVVRrfdIEVVGRSNRAPRF 480
                        250
                 ....*....|....*...
gi 158937242 491 IARLVLKSKNGIHLRLRR 508
Cdd:PLN02426 481 APGLTATVRGGLPVRVRE 498
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
115-467 3.64e-24

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: 104.80  E-value: 3.64e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 115 KSHGSY--RF-LAPWIGY--------GLLLLNGQTWFQHRRML-TPAFHYDILKPYVGLMADSVR---VMLDKWEELLGQ 179
Cdd:cd20643   31 KSEGMFpeRLsVPPWVAYrdyrkrkyGVLLKNGEAWRKDRLILnKEVLAPKVIDNFVPLLNEVSQdfvSRLHKRIKKSGS 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 180 DS-PLEVFQHVSLMTLDTIMKCAFSH-QGSIQ--VDRNSQSYIQAISdlnnLVFSRVRNAFHQNDTIYSLTSAGRWTHR- 254
Cdd:cd20643  111 GKwTADLSNDLFRFALESICNVLYGErLGLLQdyVNPEAQRFIDAIT----LMFHTTSPMLYIPPDLLRLINTKIWRDHv 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 255 -ACQLAHQHTDQVIQLRKAQLQKegelekiKRKRHLDFLDIL--LLAKmengSILSDKDLRAEVDTFMFEGHDTTASGIS 331
Cdd:cd20643  187 eAWDVIFNHADKCIQNIYRDLRQ-------KGKNEHEYPGILanLLLQ----DKLPIEDIKASVTELMAGGVDTTSMTLQ 255
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 332 WILYALATHPKHQERCREEI----HSLLGDGASItwnhLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPK 407
Cdd:cd20643  256 WTLYELARNPNVQEMLRAEVlaarQEAQGDMVKM----LKSVPLLKAAIKETLRLHPVAVSLQRYITEDLVLQNYH-IPA 330
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 408 GIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAfLPFSGGSRNCIGKQFAMNEL 467
Cdd:cd20643  331 GTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKDITHFRN-LGFGFGPRQCLGRRIAETEM 389
CYP2AB1-like cd20667
cytochrome P450, family 2, subfamily AB, polypeptide 1 and similar cytochrome P450s; The ...
130-480 1.18e-23

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


Pssm-ID: 410760 [Multi-domain]  Cd Length: 423  Bit Score: 103.38  E-value: 1.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 130 GLLLLNGQTWFQHRRmltpaFHYDILKPY-VGLMADSVRVMLDKWE--ELLGQDSPLEVFQHVSLM--TLDTIMKCAFSH 204
Cdd:cd20667   51 GIICTNGLTWKQQRR-----FCMTTLRELgLGKQALESQIQHEAAElvKVFAQENGRPFDPQDPIVhaTANVIGAVVFGH 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 205 QGSIQvDRNSQSYIQAIsdlnNLVFSRVRNAFHQndtiysLTSAGRWTHRACQLAHQHTDQVIQLRKAQLQKEGELEKIK 284
Cdd:cd20667  126 RFSSE-DPIFLELIRAI----NLGLAFASTIWGR------LYDAFPWLMRYLPGPHQKIFAYHDAVRSFIKKEVIRHELR 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 285 RKRH-LDFLDILLL----AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGA 359
Cdd:cd20667  195 TNEApQDFIDCYLAqitkTKDDPVSTFSEENMIQVVIDLFLGGTETTATTLHWALLYMVHHPEIQEKVQQELDEVLGASQ 274
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 360 SITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-- 436
Cdd:cd20667  275 LICYEDRKRLPYTNAVIHEVQRLSNVVSvGAVRQCVTSTTM-HGYYVEKGTIILPNLASVLYDPECWETPHKFNPGHFld 353
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 158937242 437 APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKV--ATALTLLRFEL 480
Cdd:cd20667  354 KDGNFVMNEAFLPFSAGHRVCLGEQLARMELFIffTTLLRTFNFQL 399
PLN02687 PLN02687
flavonoid 3'-monooxygenase
266-472 3.15e-23

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 102.97  E-value: 3.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 266 VIQLRKAQLQKEGElekikrkRHLDFLDiLLLAKMEN------GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALAT 339
Cdd:PLN02687 255 IIEEHKAAGQTGSE-------EHKDLLS-TLLALKREqqadgeGGRITDTEIKALLLNLFTAGTDTTSSTVEWAIAELIR 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 340 HPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPpvpgigrelSTPVTFP---------DGRSLPKGIM 410
Cdd:PLN02687 327 HPDILKKAQEELDAVVGRDRLVSESDLPQLTYLQAVIKETFRLHP---------STPLSLPrmaaeeceiNGYHIPKGAT 397
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158937242 411 VLLSIYGLHHNPKVWPNPEVFDPFRFAPGSaqhSHA----------FLPFSGGSRNCIGKQFAMNELKVATA 472
Cdd:PLN02687 398 LLVNVWAIARDPEQWPDPLEFRPDRFLPGG---EHAgvdvkgsdfeLIPFGAGRRICAGLSWGLRMVTLLTA 466
PLN02302 PLN02302
ent-kaurenoic acid oxidase
143-482 3.15e-23

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 102.48  E-value: 3.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 143 RRMLTPAFH-YDILKPYVGLMADSVRVMLDKWEELlgqdSPLEVFQHVSLMTLDTIMKCAFSHQGSIQVDRNSQSYiqai 221
Cdd:PLN02302 142 RRLTAAPVNgPEALSTYIPYIEENVKSCLEKWSKM----GEIEFLTELRKLTFKIIMYIFLSSESELVMEALEREY---- 213
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 222 SDLNNLVFSRVRNAfhqndtiysltsAGRWTHRACQlAHQHTDQVIQL----RKAQlQKEGELEKIKrkrhlDFLDILLL 297
Cdd:PLN02302 214 TTLNYGVRAMAINL------------PGFAYHRALK-ARKKLVALFQSivdeRRNS-RKQNISPRKK-----DMLDLLLD 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 298 AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE----IHSLLGDGASITWNHLDQMPYTT 373
Cdd:PLN02302 275 AEDENGRKLDDEEIIDLLLMYLNAGHESSGHLTMWATIFLQEHPEVLQKAKAEqeeiAKKRPPGQKGLTLKDVRKMEYLS 354
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 374 MCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQhSHAFLPFSGG 453
Cdd:PLN02302 355 QVIDETLRLINISLTVFREAKTDVEV-NGYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTPK-AGTFLPFGLG 432
                        330       340
                 ....*....|....*....|....*....
gi 158937242 454 SRNCIGKQFAMNELKVATALTLLRFELLP 482
Cdd:PLN02302 433 SRLCPGNDLAKLEISIFLHHFLLGYRLER 461
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
261-484 3.53e-23

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: 101.79  E-value: 3.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 261 QHTDQVIQLRKAQLQKEgELEKIKRKRHLDFLDILLLAKMENGsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATH 340
Cdd:cd20656  184 KHGARRDRLTKAIMEEH-TLARQKSGGGQQHFVALLTLKEQYD--LSEDTVIGLLWDMITAGMDTTAISVEWAMAEMIRN 260
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 341 PKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHH 420
Cdd:cd20656  261 PRVQEKAQEELDRVVGSDRVMTEADFPQLPYLQCVVKEALRLHPPTPLMLPHKASENVKIGGYDIPKGANVHVNVWAIAR 340
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158937242 421 NPKVWPNPEVFDPFRFAPGSAQ---HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDP 484
Cdd:cd20656  341 DPAVWKNPLEFRPERFLEEDVDikgHDFRLLPFGAGRRVCPGAQLGINLVTLMLGHLLHHFSWTPPE 407
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
324-484 3.69e-23

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 102.50  E-value: 3.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR 403
Cdd:PLN02394 307 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGNQVTEPDTHKLPYLQAVVKETLRLHMAIPLLVPHMNLEDAKLGGY 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 404 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAqHSHA------FLPFSGGSRNCIGKQFAMNELKVATALTLLR 477
Cdd:PLN02394 387 DIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEA-KVEAngndfrFLPFGVGRRSCPGIILALPILGIVLGRLVQN 465

                 ....*..
gi 158937242 478 FELLPDP 484
Cdd:PLN02394 466 FELLPPP 472
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
295-489 1.73e-22

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: 99.44  E-value: 1.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 295 LLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLlgDGASITWNHLDQMPYTTM 374
Cdd:cd20614  193 LIRARDDNGAGLSEQELVDNLRLLVLAGHETTASIMAWMVIMLAEHPAVWDALCDEAAAA--GDVPRTPAELRRFPLAEA 270
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 375 CIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFapgsAQHSHAFLP----- 449
Cdd:cd20614  271 LFRETLRLHPPVPFVFRRVLEEIEL-GGRRIPAGTHLGIPLLLFSRDPELYPDPDRFRPERW----LGRDRAPNPvellq 345
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 158937242 450 FSGGSRNCIGKQFAMNEL---KVATALTL----LRFEL---LPDPTRIPI 489
Cdd:cd20614  346 FGGGPHFCLGYHVACVELvqfIVALARELgaagIRPLLvgvLPGRRYFPT 395
CYP2W1 cd20671
cytochrome P450 family 2, subfamily W, polypeptide 1; Cytochrome P450 2W1 (CYP2W1) is ...
267-488 6.72e-22

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: 97.95  E-value: 6.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 267 IQLRKAQLQKEGELEKIKRKR------HLD------FLDILLLAKMENG---SILSDKDLRAEVDTFMFEGHDTTASGIS 331
Cdd:cd20671  165 LKLHKPILDKVEEVCMILRTLiearrpTIDgnplhsYIEALIQKQEEDDpkeTLFHDANVLACTLDLVMAGTETTSTTLQ 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 332 WILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMV 411
Cdd:cd20671  245 WAVLLMMKYPHIQKRVQEEIDRVLGPGCLPNYEDRKALPYTSAVIHEVQRFITLLPHVPRCTAADTQF-KGYLIPKGTPV 323
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158937242 412 LLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIP 488
Cdd:cd20671  324 IPLLSSVLLDKTQWETPYQFNPNHFldAEGKFVKKEAFLPFSAGRRVCVGESLARTELFIFFTGLLQKFTFLPPPGVSP 402
PLN03112 PLN03112
cytochrome P450 family protein; Provisional
273-459 1.25e-21

cytochrome P450 family protein; Provisional


Pssm-ID: 215583 [Multi-domain]  Cd Length: 514  Bit Score: 97.97  E-value: 1.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 273 QLQKEGELEKIKRKRHLDFLDILLLAKMENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEI 351
Cdd:PLN03112 258 DEHRRARSGKLPGGKDMDFVDVLLSLPGENGKEhMDDVEIKALMQDMIAAATDTSAVTNEWAMAEVIKNPRVLRKIQEEL 337
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 352 HSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV 430
Cdd:PLN03112 338 DSVVGRNRMVQESDLVHLNYLRCVVRETFRMHPAGPfLIPHESLRATTI-NGYYIPAKTRVFINTHGLGRNTKIWDDVEE 416
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 158937242 431 FDPFRFAPG-----SAQHSHAF--LPFSGGSRNCIG 459
Cdd:PLN03112 417 FRPERHWPAegsrvEISHGPDFkiLPFSAGKRKCPG 452
CYP73 cd11074
cytochrome P450 family 73; Cytochrome P450 family 73 (CYP73 pr Cyp73), also called ...
324-484 4.62e-21

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: 95.62  E-value: 4.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 324 DTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGR 403
Cdd:cd11074  247 ETTLWSIEWGIAELVNHPEIQKKLRDELDTVLGPGVQITEPDLHKLPYLQAVVKETLRLRMAIPLLVPHMNLHDAKLGGY 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 404 SLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA-----QHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRF 478
Cdd:cd11074  327 DIPAESKILVNAWWLANNPAHWKKPEEFRPERFLEEESkveanGNDFRYLPFGVGRRSCPGIILALPILGITIGRLVQNF 406

                 ....*.
gi 158937242 479 ELLPDP 484
Cdd:cd11074  407 ELLPPP 412
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
262-489 7.64e-21

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: 94.99  E-value: 7.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 262 HTDQVIQLRKAQLQKEGELEKikrkrhlDFLDILLLAKMengsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATHP 341
Cdd:cd20647  201 HVDNRLREIQKQMDRGEEVKG-------GLLTYLLVSKE-----LTLEEIYANMTEMLLAGVDTTSFTLSWATYLLARHP 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 342 KHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRelstpVTFPD----GRSLPKGIMVLLSIYG 417
Cdd:cd20647  269 EVQQQVYEEIVRNLGKRVVPTAEDVPKLPLIRALLKETLRLFPVLPGNGR-----VTQDDlivgGYLIPKGTQLALCHYS 343
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158937242 418 LHHNPKVWPNPEVFDPFRF-APGSAQHSHAF--LPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIPI 489
Cdd:cd20647  344 TSYDEENFPRAEEFRPERWlRKDALDRVDNFgsIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVSPQTTEV 418
PLN02183 PLN02183
ferulate 5-hydroxylase
264-483 1.44e-20

ferulate 5-hydroxylase


Pssm-ID: 165828 [Multi-domain]  Cd Length: 516  Bit Score: 94.92  E-value: 1.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 264 DQVIQLRKAQLQKEGELEKikrkrHLDFLDILLLAKMENGSILSDKDLRAEVD-----------TFMFEGHDTTASGISW 332
Cdd:PLN02183 252 DDHIQKRKNQNADNDSEEA-----ETDMVDDLLAFYSEEAKVNESDDLQNSIKltrdnikaiimDVMFGGTETVASAIEW 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 333 ILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPvTFPDGRSLPKGIMVL 412
Cdd:PLN02183 327 AMAELMKSPEDLKRVQQELADVVGLNRRVEESDLEKLTYLKCTLKETLRLHPPIPLLLHETAED-AEVAGYFIPKRSRVM 405
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158937242 413 LSIYGLHHNPKVWPNPEVFDPFRF----APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL-LPD 483
Cdd:PLN02183 406 INAWAIGRDKNSWEDPDTFKPSRFlkpgVPDFKGSHFEFIPFGSGRRSCPGMQLGLYALDLAVAHLLHCFTWeLPD 481
CYP2K cd20664
cytochrome P450 family 2, subfamily K; Members of CYP2K are present in fish, birds, and ...
290-510 3.13e-20

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: 92.95  E-value: 3.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLAKMEN----GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGdGASITWNH 365
Cdd:cd20664  201 GFIDAFLVKQQEEeessDSFFHDDNLTCSVGNLFGAGTDTTGTTLRWGLLLMMKYPEIQKKVQEEIDRVIG-SRQPQVEH 279
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 366 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQ 442
Cdd:cd20664  280 RKNMPYTDAVIHEIQRFANIVPmNLPHATTRDVTF-RGYFIPKGTYVIPLLTSVLQDKTEWEKPEEFNPEHFldSQGKFV 358
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158937242 443 HSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPdptriPIPIARLVLKSKNGIHLRLRRLP 510
Cdd:cd20664  359 KRDAFMPFSAGRRVCIGETLAKMELFLFFTSLLQRFRFQP-----PPGVSEDDLDLTPGLGFTLNPLP 421
CYP1D1 cd20677
cytochrome P450 family 1, subfamily D, polypeptide 1; The cytochrome P450 1D1 (CYP1D1) gene is ...
304-499 3.54e-20

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: 92.85  E-value: 3.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 304 SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLY 383
Cdd:cd20677  230 AVLSDEQIISTVNDIFGAGFDTISTALQWSLLYLIKYPEIQDKIQEEIDEKIGLSRLPRFEDRKSLHYTEAFINEVFRHS 309
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 384 PPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAF----LPFSGGSRNCIG 459
Cdd:cd20677  310 SFVPFTIPHCTTADTTLNGYFIPKDTCVFINMYQVNHDETLWKDPDLFMPERFLDENGQLNKSLvekvLIFGMGVRKCLG 389
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 158937242 460 KQFAMNELKV--ATALTLLRFELLPDPTRIPIPIARLVLKSK 499
Cdd:cd20677  390 EDVARNEIFVflTTILQQLKLEKPPGQKLDLTPVYGLTMKPK 431
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
284-479 3.76e-20

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: 92.28  E-value: 3.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 284 KRKRHL--DFLDILLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEiHSLLGDGasi 361
Cdd:cd11078  181 ERRREPrdDLISDLLAAADGDGERLTDEELVAFLFLLLVAGHETTTNLLGNAVKLLLEHPDQWRRLRAD-PSLIPNA--- 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 362 twnhldqmpyttmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfaPGSA 441
Cdd:cd11078  257 --------------VEETLRYDSPVQGLRRTATRDVEI-GGVTIPAGARVLLLFGSANRDERVFPDPDRFDIDR--PNAR 319
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 158937242 442 QHshafLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd11078  320 KH----LTFGHGIHFCLGAALARMEARIALEELLRRLP 353
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
280-492 6.44e-20

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: 91.94  E-value: 6.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 280 LEKIKRKRHL-------DFLDILLLaKM--ENGSILSD---KDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERC 347
Cdd:cd20665  185 LEKVKEHQESldvnnprDFIDCFLI-KMeqEKHNQQSEftlENLAVTVTDLFGAGTETTSTTLRYGLLLLLKHPEVTAKV 263
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 348 REEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWP 426
Cdd:cd20665  264 QEEIDRVIGRHRSPCMQDRSHMPYTDAVIHEIQRYIDLVPnNLPHAVTCDTKF-RNYLIPKGTTVITSLTSVLHDDKEFP 342
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 158937242 427 NPEVFDPFRF--APGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLP--DPTRIPI-PIA 492
Cdd:cd20665  343 NPEKFDPGHFldENGNFKKSDYFMPFSAGKRICAGEGLARMELFLFLTTILQNFNLKSlvDPKDIDTtPVV 413
CYP_TRI13-like cd20622
fungal cytochrome P450s similar to TRI13; This subfamily is composed of cytochrome P450 ...
135-487 8.05e-20

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: 92.36  E-value: 8.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 135 NGQTWFQHRRML----TPAFHYDILKPYvglMADSVRVMLDKWEE--LLGQDSPLEVFQHVSLMTLDTIMKCAFshqGSI 208
Cdd:cd20622   58 TGPAFRKHRSLVqdlmTPSFLHNVAAPA---IHSKFLDLIDLWEAkaRLAKGRPFSAKEDIHHAALDAIWAFAF---GIN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 209 QVDRNSQSYIQAISDLNNLV---------------FSRVRNAFHQ-NDTI-YSLTSagrWTHRacqLAHQHTDQVIQLRK 271
Cdd:cd20622  132 FDASQTRPQLELLEAEDSTIlpagldepvefpeapLPDELEAVLDlADSVeKSIKS---PFPK---LSHWFYRNQPSYRR 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 272 AQLQKE----GELEKIKRKRHLDFLDI-------------LLLAKMENGSILSDKD-LRAEVDTFMFEGHDTTASGISWI 333
Cdd:cd20622  206 AAKIKDdflqREIQAIARSLERKGDEGevrsavdhmvrreLAAAEKEGRKPDYYSQvIHDELFGYLIAGHDTTSTALSWG 285
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 334 LYALATHPKHQERCREEIHSLL----GDGASITWNHLDQM--PYTTMCIKEALRLYPPVPGIGRELSTPVTFPdGRSLPK 407
Cdd:cd20622  286 LKYLTANQDVQSKLRKALYSAHpeavAEGRLPTAQEIAQAriPYLDAVIEEILRCANTAPILSREATVDTQVL-GYSIPK 364
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 408 GIMVLL-------------------SIYGLHHNPKVW----PNPEVFDPFR------------FAPGSAQHshafLPFSG 452
Cdd:cd20622  365 GTNVFLlnngpsylsppieidesrrSSSSAAKGKKAGvwdsKDIADFDPERwlvtdeetgetvFDPSAGPT----LAFGL 440
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 158937242 453 GSRNCIGKQFAMNELKVATALTLLRFELLPDPTRI 487
Cdd:cd20622  441 GPRGCFGRRLAYLEMRLIITLLVWNFELLPLPEAL 475
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
332-484 1.26e-19

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: 90.83  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 332 WILYALATHPKHQERCREEIHSLLGDG----ASITWNHLDQMPYTTMCIKEALRLYPPvpG-IGRELSTPVTFPDgRSLP 406
Cdd:cd20635  232 WTLAFILSHPSVYKKVMEEISSVLGKAgkdkIKISEDDLKKMPYIKRCVLEAIRLRSP--GaITRKVVKPIKIKN-YTIP 308
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 407 KGIMVLLSIYGLHHNPKVWPNPEVFDPFR----------FAPGsaqhshaFLPFSGGSRNCIGKQFAMNELKVATALTLL 476
Cdd:cd20635  309 AGDMLMLSPYWAHRNPKYFPDPELFKPERwkkadleknvFLEG-------FVAFGGGRYQCPGRWFALMEIQMFVAMFLY 381
                        170
                 ....*....|...
gi 158937242 477 RFEL-----LPDP 484
Cdd:cd20635  382 KYDFtlldpVPKP 394
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
290-488 1.99e-19

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: 90.83  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLA-----KMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDG--ASIT 362
Cdd:cd20675  210 DMMDAFILAlekgkSGDSGVGLDKEYVPSTVTDIFGASQDTLSTALQWILLLLVRYPDVQARLQEELDRVVGRDrlPCIE 289
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 363 wnhlDQ--MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--AP 438
Cdd:cd20675  290 ----DQpnLPYVMAFLYEAMRFSSFVPVTIPHATTADTSILGYHIPKDTVVFVNQWSVNHDPQKWPNPEVFDPTRFldEN 365
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158937242 439 GSAQHSHAF--LPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRIP 488
Cdd:cd20675  366 GFLNKDLASsvMIFSVGKRRCIGEELSKMQLFLFTSILAHQCNFTANPNEPL 417
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
285-489 3.88e-19

cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial CYPs similar to Agrobacterium tumefaciens plant-inducible cytochrome P450-pinF1, which is not essential for virulence but may be involved in the detoxification of plant protective agents at the site of wounding. The P450-pinF1-like subfamily belongs to the large cytochrome P450 (P450, CYP) superfamily of heme-containing proteins that catalyze a variety of oxidative reactions of a large number of structurally different endogenous and exogenous compounds in organisms from all major domains of life. CYPs bind their diverse ligands in a buried, hydrophobic active site, which is accessed through a substrate access channel formed by two flexible helices and their connecting loop.


Pssm-ID: 410722 [Multi-domain]  Cd Length: 353  Bit Score: 88.90  E-value: 3.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 285 RKRHL--DFLDILLLAKMEnGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEiHSLLGdgasit 362
Cdd:cd20629  166 RRRAPgdDLISRLLRAEVE-GEKLDDEEIISFLRLLLPAGSDTTYRALANLLTLLLQHPEQLERVRRD-RSLIP------ 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 363 wnhldqmpyttMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsAQ 442
Cdd:cd20629  238 -----------AAIEEGLRWEPPVASVPRMALRDVEL-DGVTIPAGSLLDLSVGSANRDEDVYPDPDVFDIDR-----KP 300
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 158937242 443 HSHafLPFSGGSRNCIGKQFAMNELKVATALTLLRF---ELLPDPTRIPI 489
Cdd:cd20629  301 KPH--LVFGGGAHRCLGEHLARVELREALNALLDRLpnlRLDPDAPAPEI 348
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
290-482 3.88e-19

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: 89.82  E-value: 3.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLlAKM--ENGSILS---DKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 364
Cdd:cd20669  202 DFIDCFL-TKMaeEKQDPLShfnMETLVMTTHNLLFGGTETVSTTLRYGFLILMKYPKVAARVQEEIDRVVGRNRLPTLE 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 365 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 441
Cdd:cd20669  281 DRARMPYTDAVIHEIQRFADIIPmSLPHAVTRDTNF-RGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFldDNGSF 359
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158937242 442 QHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLP 482
Cdd:cd20669  360 KKNDAFMPFSAGKRICLGESLARMELFLYLTAILQNFSLQP 400
CYP_GliC-like cd20615
cytochrome P450 monooxygenases similar to gliotoxin biosynthesis protein C; This subfamily is ...
90-482 5.12e-19

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: 89.27  E-value: 5.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242  90 LWGGKVR-VQLYDPDYMKVILGRSDpKSHGSYRFLAPW-----IGYGLLLLNGQTWFQHRRMLTPAFHYDILKPYVGLMA 163
Cdd:cd20615    6 IWSGPTPeIVLTTPEHVKEFYRDSN-KHHKAPNNNSGWlfgqlLGQCVGLLSGTDWKRVRKVFDPAFSHSAAVYYIPQFS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 164 DSVRvmldKWEELLGQDSP------LEVFQHVSLMTLDTIMKCAFshqGSIqvdrnSQSYIQAISDLNNL-------VFS 230
Cdd:cd20615   85 REAR----KWVQNLPTNSGdgrrfvIDPAQALKFLPFRVIAEILY---GEL-----SPEEKEELWDLAPLreelfkyVIK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 231 RVRNAFhqndTIYSL--TSAGRwthracQLAHQHTDQVIQLRKAQlqkegeleKIKRKRHLDFLDILLLAKMENGSIlSD 308
Cdd:cd20615  153 GGLYRF----KISRYlpTAANR------RLREFQTRWRAFNLKIY--------NRARQRGQSTPIVKLYEAVEKGDI-TF 213
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 309 KDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHL-DQMPYTTMCIKEALRLYPpvp 387
Cdd:cd20615  214 EELLQTLDEMLFANLDVTTGVLSWNLVFLAANPAVQEKLREEISAAREQSGYPMEDYIlSTDTLLAYCVLESLRLRP--- 290
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 388 gigrelSTPVTFP---------DGRSLPKGIMVLLSIYGLHHN-PKVWPNPEVFDPFRFA-PGSAQHSHAFLPFSGGSRN 456
Cdd:cd20615  291 ------LLAFSVPessptdkiiGGYRIPANTPVVVDTYALNINnPFWGPDGEAYRPERFLgISPTDLRYNFWRFGFGPRK 364
                        410       420
                 ....*....|....*....|....*.
gi 158937242 457 CIGKQFAMNELKVATALTLLRFELLP 482
Cdd:cd20615  365 CLGQHVADVILKALLAHLLEQYELKL 390
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
261-467 1.84e-18

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: 87.59  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 261 QHTDQVIQLRKAQLQkegelekIKRKRHLDFLDILLLAKMEngsiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATH 340
Cdd:cd20644  194 QYADNCIQKIYQELA-------FGRPQHYTGIVAELLLQAE----LSLEAIKANITELTAGGVDTTAFPLLFTLFELARN 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 341 PKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHH 420
Cdd:cd20644  263 PDVQQILRQESLAAAAQISEHPQKALTELPLLKAALKETLRLYPVGITVQRVPSSDLVLQNYH-IPAGTLVQVFLYSLGR 341
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 158937242 421 NPKVWPNPEVFDPFRFAP--GSAQHSHAfLPFSGGSRNCIGKQFAMNEL 467
Cdd:cd20644  342 SAALFPRPERYDPQRWLDirGSGRNFKH-LAFGFGMRQCLGRRLAEAEM 389
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
135-487 2.45e-18

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: 87.03  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 135 NGQTWFQHRRMLTPAFHYDILKPYVGLMADSVRVMLDKWEELLGQDSplevfqHVSLMTLdtiMKCafshqgsIQVDRNS 214
Cdd:cd20616   66 NPALWKKVRPFFAKALTGPGLVRMVTVCVESTNTHLDNLEEVTNESG------YVDVLTL---MRR-------IMLDTSN 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 215 QSYIQAISDLNNLVFsRVRNAFH-------QNDTIYSLtsagRWTHRACQLAHQHTDQVI-----QLRKAQLQKEgelek 282
Cdd:cd20616  130 RLFLGVPLNEKAIVL-KIQGYFDawqalliKPDIFFKI----SWLYKKYEKAVKDLKDAIeilieQKRRRISTAE----- 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 283 iKRKRHLDFLDILLLAkmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDgASIT 362
Cdd:cd20616  200 -KLEDHMDFATELIFA--QKRGELTAENVNQCVLEMLIAAPDTMSVSLFFMLLLIAQHPEVEEAILKEIQTVLGE-RDIQ 275
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 363 WNHLDQMPYTTMCIKEALRLYPPVPGIGRE-LSTPVTfpDGRSLPKGIMVLLSIyGLHHNPKVWPNPEVFDPFRFA---P 438
Cdd:cd20616  276 NDDLQKLKVLENFINESMRYQPVVDFVMRKaLEDDVI--DGYPVKKGTNIILNI-GRMHRLEFFPKPNEFTLENFEknvP 352
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 158937242 439 gsaqhSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDPTRI 487
Cdd:cd20616  353 -----SRYFQPFGFGPRSCVGKYIAMVMMKAILVTLLRRFQVCTLQGRC 396
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
319-464 4.41e-18

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: 86.50  E-value: 4.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 319 MFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVT 398
Cdd:cd20653  236 LLAGTDTSAVTLEWAMSNLLNHPEVLKKAREEIDTQVGQDRLIEESDLPKLPYLQNIISETLRLYPAAPLLVPHESSEDC 315
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 158937242 399 FPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFLPFSGGSRNCIGKQFAM 464
Cdd:cd20653  316 KIGGYDIPRGTMLLVNAWAIHRDPKLWEDPTKFKPERFE-GEEREGYKLIPFGLGRRACPGAGLAQ 380
Cyp158A-like cd11031
cytochrome P450 family 158, subfamily A and similar cytochrome P450s; This family is composed ...
250-510 5.12e-18

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


Pssm-ID: 410657 [Multi-domain]  Cd Length: 380  Bit Score: 85.69  E-value: 5.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 250 RWTHRACQLAHqHTDQVIQLRKAQLQKE-GELEKIKRKRHLDflDIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTT 326
Cdd:cd11031  146 AWSDALLSTSA-LTPEEAEAARQELRGYmAELVAARRAEPGD--DLLsaLVAARDDDDRLSEEELVTLAVGLLVAGHETT 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 327 ASGISWILYALATHPKHQERCREEiHSLLGDGasitwnhldqmpyttmcIKEALRLYPPVPGIG--RELSTPVTFPDGRs 404
Cdd:cd11031  223 ASQIGNGVLLLLRHPEQLARLRAD-PELVPAA-----------------VEELLRYIPLGAGGGfpRYATEDVELGGVT- 283
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 405 LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapGSAQHshafLPFSGGSRNCIGKQFAMNELKVATALTLLRFellpdP 484
Cdd:cd11031  284 IRAGEAVLVSLNAANRDPEVFPDPDRLDLDR---EPNPH----LAFGHGPHHCLGAPLARLELQVALGALLRRL-----P 351
                        250       260
                 ....*....|....*....|....*..
gi 158937242 485 T-RIPIPIARLVLKSKNGIHlRLRRLP 510
Cdd:cd11031  352 GlRLAVPEEELRWREGLLTR-GPEELP 377
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
129-493 1.11e-17

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 85.42  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 129 YGLLLLNGQTwfqHRRM--LTPAF-HYDILKPYVGLMADS-VRVMLDKWEellgqdSPLEVFQHVSLMTLDTIMKCAFSH 204
Cdd:PLN02987 115 HSLLLMKGNL---HKKMhsLTMSFaNSSIIKDHLLLDIDRlIRFNLDSWS------SRVLLMEEAKKITFELTVKQLMSF 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 205 QGSIQVDRNSQSYIQAISDLNNLVFSrvrnafhqndtIYSLTsagrwTHRACQlAHQHTDQVIQLRKAQLQKEGElEKIK 284
Cdd:PLN02987 186 DPGEWTESLRKEYVLVIEGFFSVPLP-----------LFSTT-----YRRAIQ-ARTKVAEALTLVVMKRRKEEE-EGAE 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 285 RKRhlDFLDILLLAkmenGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE---IHSLLGDGASI 361
Cdd:PLN02987 248 KKK--DMLAALLAS----DDGFSDEEIVDFLVALLVAGYETTSTIMTLAVKFLTETPLALAQLKEEhekIRAMKSDSYSL 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 362 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA--PG 439
Cdd:PLN02987 322 EWSDYKSMPFTQCVVNETLRVANIIGGIFRRAMTDIEV-KGYTIPKGWKVFASFRAVHLDHEYFKDARTFNPWRWQsnSG 400
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158937242 440 SAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPD--------PT-----RIPIPIAR 493
Cdd:PLN02987 401 TTVPSNVFTPFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPAeqdklvffPTtrtqkRYPINVKR 467
PLN02971 PLN02971
tryptophan N-hydroxylase
261-489 1.67e-17

tryptophan N-hydroxylase


Pssm-ID: 166612 [Multi-domain]  Cd Length: 543  Bit Score: 85.47  E-value: 1.67e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 261 QHTDQVIQLRkAQLQKEGelekiKRKRHLDFLDILLLAKMENGS-ILSDKDLRAEVDTFMFEGHDTTASGISWILYALAT 339
Cdd:PLN02971 283 KYHDPIIDER-IKMWREG-----KRTQIEDFLDIFISIKDEAGQpLLTADEIKPTIKELVMAAPDNPSNAVEWAMAEMIN 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 340 HPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLH 419
Cdd:PLN02971 357 KPEILHKAMEEIDRVVGKERFVQESDIPKLNYVKAIIREAFRLHPVAAFNLPHVALSDTTVAGYHIPKGSQVLLSRYGLG 436
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 158937242 420 HNPKVWPNPEVFDPFRFAPGSA-----QHSHAFLPFSGGSRNCIGKQF--AMNELKVATALTLLRFELLPDPTRIPI 489
Cdd:PLN02971 437 RNPKVWSDPLSFKPERHLNECSevtltENDLRFISFSTGKRGCAAPALgtAITTMMLARLLQGFKWKLAGSETRVEL 513
PLN00110 PLN00110
flavonoid 3',5'-hydroxylase (F3'5'H); Provisional
284-464 1.68e-17

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


Pssm-ID: 177725  Cd Length: 504  Bit Score: 85.29  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 284 KRKRHLDFLDILLlAKMEN--GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASI 361
Cdd:PLN00110 262 ERKGNPDFLDVVM-ANQENstGEKLTLTNIKALLLNLFTAGTDTSSSVIEWSLAEMLKNPSILKRAHEEMDQVIGRNRRL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 362 TWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 441
Cdd:PLN00110 341 VESDLPKLPYLQAICKESFRKHPSTPLNLPRVSTQACEVNGYYIPKNTRLSVNIWAIGRDPDVWENPEEFRPERFLSEKN 420
                        170       180
                 ....*....|....*....|....*....
gi 158937242 442 Q------HSHAFLPFSGGSRNCIGKQFAM 464
Cdd:PLN00110 421 AkidprgNDFELIPFGAGRRICAGTRMGI 449
PLN02774 PLN02774
brassinosteroid-6-oxidase
267-506 3.71e-17

brassinosteroid-6-oxidase


Pssm-ID: 178373 [Multi-domain]  Cd Length: 463  Bit Score: 84.06  E-value: 3.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 267 IQLRKAQLQKEGELEKIKRKRHLDFLDIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 344
Cdd:PLN02774 219 VQARKNIVRMLRQLIQERRASGETHTDMLgyLMRKEGNRYKLTDEEIIDQIITILYSGYETVSTTSMMAVKYLHDHPKAL 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 345 ERCREEiHSLLGDGAS----ITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHH 420
Cdd:PLN02774 299 QELRKE-HLAIRERKRpedpIDWNDYKSMRFTRAVIFETSRLATIVNGVLRKTTQDMEL-NGYVIPKGWRIYVYTREINY 376
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 421 NPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNElkVATAL----TLLRFELLPDPTRIPIPiarlVL 496
Cdd:PLN02774 377 DPFLYPDPMTFNPWRWLDKSLESHNYFFLFGGGTRLCPGKELGIVE--ISTFLhyfvTRYRWEEVGGDKLMKFP----RV 450
                        250
                 ....*....|
gi 158937242 497 KSKNGIHLRL 506
Cdd:PLN02774 451 EAPNGLHIRV 460
CYP164-like cd20625
cytochrome P450 family 164 and similar cytochrome P450s; This group is composed mostly of ...
293-510 7.08e-17

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: 82.21  E-value: 7.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 293 DIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREeihsllgdgasitwnHLDQMP 370
Cdd:cd20625  182 DLIsaLVAAEEDGDRLSEDELVANCILLLVAGHETTVNLIGNGLLALLRHPEQLALLRA---------------DPELIP 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 371 YTtmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSaqhshafLPF 450
Cdd:cd20625  247 AA---VEELLRYDSPVQLTARVALEDVEI-GGQTIPAGDRVLLLLGAANRDPAVFPDPDRFDITRAPNRH-------LAF 315
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158937242 451 SGGSRNCIGKQFAMNELKVA-TALtllrFELLPDPTRIPIPIARlvlksKNGIHLR-LRRLP 510
Cdd:cd20625  316 GAGIHFCLGAPLARLEAEIAlRAL----LRRFPDLRLLAGEPEW-----RPSLVLRgLRSLP 368
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
285-493 7.15e-17

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: 82.09  E-value: 7.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 285 RKRHL---DFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEiHSLLGDGasi 361
Cdd:cd20630  176 RRQAPvedDLLTTLLRAE-EDGERLSEDELMALVAALIVAGTDTTVHLITFAVYNLLKHPEALRKVKAE-PELLRNA--- 250
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 362 twnhldqmpyttmcIKEALRLyppvPGIGRELSTPVTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfa 437
Cdd:cd20630  251 --------------LEEVLRW----DNFGKMGTARYATEDvelcGVTIRKGQMVLLLLPSALRDEKVFSDPDRFDVRR-- 310
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 158937242 438 pgsaqHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRF---ELLPDPTRIPIPIAR 493
Cdd:cd20630  311 -----DPNANIAFGYGPHFCIGAALARLELELAVSTLLRRFpemELAEPPVFDPHPVLR 364
CYP_unk cd20624
unknown subfamily of actinobacterial cytochrome P450s; This subfamily is composed of ...
327-494 8.83e-17

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: 82.12  E-value: 8.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 327 ASGISWI--LYALATHPKHQERCREEIHSLLGDGAsitwnhldqMPYTTMCIKEALRLYPPVPGIGRELSTPvTFPDGRS 404
Cdd:cd20624  206 AAGMALLraLALLAAHPEQAARAREEAAVPPGPLA---------RPYLRACVLDAVRLWPTTPAVLRESTED-TVWGGRT 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 405 LPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLPDP 484
Cdd:cd20624  276 VPAGTGFLIFAPFFHRDDEALPFADRFVPEIWLDGRAQPDEGLVPFSAGPARCPGENLVLLVASTALAALLRRAEIDPLE 355
                        170
                 ....*....|
gi 158937242 485 TRIPIPIARL 494
Cdd:cd20624  356 SPRSGPGEPL 365
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
290-467 1.20e-16

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: 82.15  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLAKMEN----GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNH 365
Cdd:cd20668  202 DFIDSFLIRMQEEkknpNTEFYMKNLVMTTLNLFFAGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGRNRQPKFED 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 366 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFA--PGSAQ 442
Cdd:cd20668  282 RAKMPYTEAVIHEIQRFGDVIPmGLARRVTKDTKF-RDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFLddKGQFK 360
                        170       180
                 ....*....|....*....|....*
gi 158937242 443 HSHAFLPFSGGSRNCIGKQFAMNEL 467
Cdd:cd20668  361 KSDAFVPFSIGKRYCFGEGLARMEL 385
CYP134A1 cd11080
cytochrome P450 family 134, subfamily A, polypeptide 1; Cytochrome P450 134A1 (CYP134A1, EC 1. ...
268-479 1.76e-16

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: 80.98  E-value: 1.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 268 QLRKAQLQKEGELEKIK-RKRH--LDFLDILLLAKMeNGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 344
Cdd:cd11080  149 GLRCAEQLSQYLLPVIEeRRVNpgSDLISILCTAEY-EGEALSDEDIKALILNVLLAATEPADKTLALMIYHLLNNPEQL 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 345 ERCREEiHSLLgdgasitwnhldqmpytTMCIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLLSIYGLHHNPKV 424
Cdd:cd11080  228 AAVRAD-RSLV-----------------PRAIAETLRYHPPVQLIPRQASQDVVVSGME-IKKGTTVFCLIGAANRDPAA 288
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 158937242 425 WPNPEVFDPFR--------FAPgSAQHshafLPFSGGSRNCIGKQFAMNELKVATALTL-----LRFE 479
Cdd:cd11080  289 FEDPDTFNIHRedlgirsaFSG-AADH----LAFGSGRHFCVGAALAKREIEIVANQVLdalpnIRLE 351
PLN02169 PLN02169
fatty acid (omega-1)-hydroxylase/midchain alkane hydroxylase
307-508 3.99e-16

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


Pssm-ID: 177826 [Multi-domain]  Cd Length: 500  Bit Score: 80.82  E-value: 3.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 307 SDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDgasitwNHLDQMPYTTMCIKEALRLYPPV 386
Cdd:PLN02169 298 KDKFIRDVIFSLVLAGRDTTSSALTWFFWLLSKHPQVMAKIRHEINTKFDN------EDLEKLVYLHAALSESMRLYPPL 371
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 387 PGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEV-FDPFRFAP--GSAQH--SHAFLPFSGGSRNCIGKQ 461
Cdd:PLN02169 372 PFNHKAPAKPDVLPSGHKVDAESKIVICIYALGRMRSVWGEDALdFKPERWISdnGGLRHepSYKFMAFNSGPRTCLGKH 451
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 158937242 462 FAMNELKVaTALTLLR---FELLPDPTRIPIPiaRLVLKSKNGIHLRLRR 508
Cdd:PLN02169 452 LALLQMKI-VALEIIKnydFKVIEGHKIEAIP--SILLRMKHGLKVTVTK 498
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
290-482 6.36e-16

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: 79.97  E-value: 6.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLaKM--ENGSILSDKDLRAEVDT---FMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 364
Cdd:cd20670  202 DFIDCFLI-KMhqDKNNPHTEFNLKNLVLTtlnLFFAGTETVSSTLRYGFLLLMKYPEVEAKIHEEINQVIGPHRLPSVD 280
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 365 HLDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA 441
Cdd:cd20670  281 DRVKMPYTDAVIHEIQRLTDIVPlGVPHNVIRDTQF-RGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFldEQGRF 359
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158937242 442 QHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFELLP 482
Cdd:cd20670  360 KKNEAFVPFSSGKRVCLGEAMARMELFLYFTSILQNFSLRS 400
CYP2D cd20663
cytochrome P450 family 2, subfamily D; Members of CYP2D are present in mammals, birds, ...
290-467 1.76e-15

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: 78.58  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLlAKMENG-----SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWN 364
Cdd:cd20663  206 DLTDAFL-AEMEKAkgnpeSSFNDENLRLVVADLFSAGMVTTSTTLSWALLLMILHPDVQRRVQQEIDEVIGQVRRPEMA 284
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 365 HLDQMPYTTMCIKEALRLYPPVPgigreLSTP-VTFPD----GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--A 437
Cdd:cd20663  285 DQARMPYTNAVIHEVQRFGDIVP-----LGVPhMTSRDievqGFLIPKGTTLITNLSSVLKDETVWEKPLRFHPEHFldA 359
                        170       180       190
                 ....*....|....*....|....*....|
gi 158937242 438 PGSAQHSHAFLPFSGGSRNCIGKQFAMNEL 467
Cdd:cd20663  360 QGHFVKPEAFMPFSAGRRACLGEPLARMEL 389
CYP1A cd20676
cytochrome P450 family 1, subfamily A; Cytochrome P450 family 1, subfamily A (CYP1A) consists ...
301-499 1.86e-15

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: 78.52  E-value: 1.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 301 ENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEA 379
Cdd:cd20676  227 ENANIqLSDEKIVNIVNDLFGAGFDTVTTALSWSLMYLVTYPEIQKKIQEELDEVIGRERRPRLSDRPQLPYLEAFILET 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 380 LRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSA---QHSHAFLPFSGGS 454
Cdd:cd20676  307 FRHSSFVPFTIPHCTTRDTSLNGYYIPKDTCVFINQWQVNHDEKLWKDPSSFRPERFltADGTEinkTESEKVMLFGLGK 386
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 158937242 455 RNCIGKQFAMNE--LKVATALTLLRFELLP----DPTripiPIARLVLKSK 499
Cdd:cd20676  387 RRCIGESIARWEvfLFLAILLQQLEFSVPPgvkvDMT----PEYGLTMKHK 433
CYP2B cd20672
cytochrome P450 family 2, subfamily B; The human cytochrome P450 family 2, subfamily B (CYP2B) ...
290-467 3.42e-15

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: 77.51  E-value: 3.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLL----AKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNH 365
Cdd:cd20672  202 DFIDTYLLrmekEKSNHHTEFHHQNLMISVLSLFFAGTETTSTTLRYGFLLMLKYPHVAEKVQKEIDQVIGSHRLPTLDD 281
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 366 LDQMPYTTMCIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF--APGSAQ 442
Cdd:cd20672  282 RAKMPYTDAVIHEIQRFSDLIPiGVPHRVTKDTLF-RGYLLPKNTEVYPILSSALHDPQYFEQPDTFNPDHFldANGALK 360
                        170       180
                 ....*....|....*....|....*
gi 158937242 443 HSHAFLPFSGGSRNCIGKQFAMNEL 467
Cdd:cd20672  361 KSEAFMPFSTGKRICLGEGIARNEL 385
PLN03018 PLN03018
homomethionine N-hydroxylase
256-478 5.18e-15

homomethionine N-hydroxylase


Pssm-ID: 178592 [Multi-domain]  Cd Length: 534  Bit Score: 77.74  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 256 CQLAHQHTDQVIQLRKAQLQKEGELEKIKrkrhlDFLDILLLAKMENGSILSDKD-LRAEVDTFMFEGHDTTASGISWIL 334
Cdd:PLN03018 264 VNLVRSYNNPIIDERVELWREKGGKAAVE-----DWLDTFITLKDQNGKYLVTPDeIKAQCVEFCIAAIDNPANNMEWTL 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 335 YALATHPKHQERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLS 414
Cdd:PLN03018 339 GEMLKNPEILRKALKELDEVVGKDRLVQESDIPNLNYLKACCRETFRIHPSAHYVPPHVARQDTTLGGYFIPKGSHIHVC 418
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 158937242 415 IYGLHHNPKVWPNPEVFDPFRFAPGSA--------QHSHAFLPFSGGSRNCIGkqfamneLKVAT---ALTLLRF 478
Cdd:PLN03018 419 RPGLGRNPKIWKDPLVYEPERHLQGDGitkevtlvETEMRFVSFSTGRRGCVG-------VKVGTimmVMMLARF 486
PLN00168 PLN00168
Cytochrome P450; Provisional
270-479 6.11e-15

Cytochrome P450; Provisional


Pssm-ID: 215086 [Multi-domain]  Cd Length: 519  Bit Score: 77.30  E-value: 6.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 270 RKAQLQKEGELEKIKRKRHLDFLDILLLAKM--ENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERC 347
Cdd:PLN00168 264 YKNHLGQGGEPPKKETTFEHSYVDTLLDIRLpeDGDRALTDDEIVNLCSEFLNAGTDTTSTALQWIMAELVKNPSIQSKL 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 348 REEIHSLLGDGA-SITWNHLDQMPYTTMCIKEALRLYPP----VPGIGRElstpvtfpD----GRSLPKGIMVLLSIYGL 418
Cdd:PLN00168 344 HDEIKAKTGDDQeEVSEEDVHKMPYLKAVVLEGLRKHPPahfvLPHKAAE--------DmevgGYLIPKGATVNFMVAEM 415
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 158937242 419 HHNPKVWPNPEVFDPFRFAPG--------SAQHSHAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:PLN00168 416 GRDEREWERPMEFVPERFLAGgdgegvdvTGSREIRMMPFGVGRRICAGLGIAMLHLEYFVANMVREFE 484
CYP152 cd11067
cytochrome P450 family 152, also called fatty acid hydroxylases or P450 peroxygenases; The ...
330-497 6.29e-15

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: 76.41  E-value: 6.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 330 ISWILYALATHPKHQERCREeihsllgdgasitwnhlDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGI 409
Cdd:cd11067  240 VTFAALALHEHPEWRERLRS-----------------GDEDYAEAFVQEVRRFYPFFPFVGARARRDFEW-QGYRFPKGQ 301
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 410 MVLLSIYGLHHNPKVWPNPEVFDPFRFApGSAQHSHAFLPFSGGSRN----CIGKQFAMNELKVATA-LTLLRFELLPDP 484
Cdd:cd11067  302 RVLLDLYGTNHDPRLWEDPDRFRPERFL-GWEGDPFDFIPQGGGDHAtghrCPGEWITIALMKEALRlLARRDYYDVPPQ 380
                        170       180
                 ....*....|....*....|
gi 158937242 485 ------TRIP-IPIARLVLK 497
Cdd:cd11067  381 dlsidlNRMPaLPRSGFVIR 400
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
322-488 2.48e-14

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: 74.54  E-value: 2.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 322 GHDTTASGISWILYALATHPKHQERCREEiHSLLgdgasitwnhldqmpytTMCIKEALRLYPPVPGIGRELSTPVTFpD 401
Cdd:cd11037  214 GLDTTISAIGNALWLLARHPDQWERLRAD-PSLA-----------------PNAFEEAVRLESPVQTFSRTTTRDTEL-A 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 402 GRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApgsAQHshafLPFSGGSRNCIGKQFAMNELK-VATALTLL--RF 478
Cdd:cd11037  275 GVTIPAGSRVLVFLGSANRDPRKWDDPDRFDITRNP---SGH----VGFGHGVHACVGQHLARLEGEaLLTALARRvdRI 347
                        170
                 ....*....|
gi 158937242 479 ELLPDPTRIP 488
Cdd:cd11037  348 ELAGPPVRAL 357
CYP20A1 cd20627
cytochrome P450 family 20, subfamily A, polypeptide 1; Cytochrome P450, family 20, subfamily A, ...
268-482 3.64e-14

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: 74.08  E-value: 3.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 268 QLRKAQLQKEGELEKIKRKR------HLDFLDILLLAKMENGSILSDKDLraevdtFMFEGHDTTASGISWILYALATHP 341
Cdd:cd20627  160 QYEDALMEMESVLKKVIKERkgknfsQHVFIDSLLQGNLSEQQVLEDSMI------FSLAGCVITANLCTWAIYFLTTSE 233
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 342 KHQERCREEIHSLLGDGAsITWNHLDQMPYTTMCIKEALRL--YPPVPGIGRELSTPVtfpDGRSLPKGIMVLLSIYGLH 419
Cdd:cd20627  234 EVQKKLYKEVDQVLGKGP-ITLEKIEQLRYCQQVLCETVRTakLTPVSARLQELEGKV---DQHIIPKETLVLYALGVVL 309
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158937242 420 HNPKVWPNPEVFDPFRFAPGSAQHSHAFLPFSgGSRNCIGKQFAMNELKVATALTLLRFELLP 482
Cdd:cd20627  310 QDNTTWPLPYRFDPDRFDDESVMKSFSLLGFS-GSQECPELRFAYMVATVLLSVLVRKLRLLP 371
CYP107-like cd11029
cytochrome P450 family 107 and similar cytochrome P450s; This group contains bacterial ...
290-510 1.80e-13

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: 71.79  E-value: 1.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLlgDGAsitwnhldqm 369
Cdd:cd11029  192 DLLSALVAAR-DEGDRLSEEELVSTVFLLLVAGHETTVNLIGNGVLALLTHPDQLALLRADPELW--PAA---------- 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 370 pyttmcIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapGSAQHshafL 448
Cdd:cd11029  259 ------VEELLRYDGPVAlATLRFATEDVEV-GGVTIPAGEPVLVSLAAANRDPARFPDPDRLDITR---DANGH----L 324
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 158937242 449 PFSGGSRNCIGKQFAMNELKVatALTLLrFELLPDpTRIPIPIARLVLKSKNGIHlRLRRLP 510
Cdd:cd11029  325 AFGHGIHYCLGAPLARLEAEI--ALGAL-LTRFPD-LRLAVPPDELRWRPSFLLR-GLRALP 381
P450cin-like cd11034
P450cin and similar cytochrome P450s; This group is composed of Citrobacter braakii cytochrome ...
290-485 2.39e-13

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: 71.60  E-value: 2.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLAKMeNGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPkhQERCReeihsLLGDGASItwnhldqm 369
Cdd:cd11034  171 DLISRLIEGEI-DGKPLSDGEVIGFLTLLLLGGTDTTSSALSGALLWLAQHP--EDRRR-----LIADPSLI-------- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 370 pytTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFApgsaqHSHafLP 449
Cdd:cd11034  235 ---PNAVEEFLRFYSPVAGLARTVTQEVEV-GGCRLKPGDRVLLAFASANRDEEKFEDPDRIDIDRTP-----NRH--LA 303
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 158937242 450 FSGGSRNCIGKQFAMNELKVATALTLLR---FELLPDPT 485
Cdd:cd11034  304 FGSGVHRCLGSHLARVEARVALTEVLKRipdFELDPGAT 342
PLN02966 PLN02966
cytochrome P450 83A1
310-483 5.81e-13

cytochrome P450 83A1


Pssm-ID: 178550 [Multi-domain]  Cd Length: 502  Bit Score: 70.93  E-value: 5.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 310 DLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGAS--ITWNHLDQMPYTTMCIKEALRLYPPVP 387
Cdd:PLN02966 289 NVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGStfVTEDDVKNLPYFRALVKETLRIEPVIP 368
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 388 GIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQHS---HAFLPFSGGSRNCIGKQFA 463
Cdd:PLN02966 369 LLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWgPNPDEFRPERFLEKEVDFKgtdYEFIPFGSGRRMCPGMRLG 448
                        170       180
                 ....*....|....*....|.
gi 158937242 464 MNELKVATALTLLRFEL-LPD 483
Cdd:PLN02966 449 AAMLEVPYANLLLNFNFkLPN 469
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
254-486 8.53e-13

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: 69.70  E-value: 8.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 254 RACQLAHQHTDQVIQLRKAQLQKegelekikrkrhlDFLDILLLAKmENGSILSDKDLRAEVDTFMFEGHDTTASGISWI 333
Cdd:cd11038  172 AAVEELYDYADALIEARRAEPGD-------------DLISTLVAAE-QDGDRLSDEELRNLIVALLFAGVDTTRNQLGLA 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 334 LYALATHPKHQERCREeiHSLLGDGAsitwnhldqmpyttmcIKEALRLYPPVPGIGRELSTPVTFPDGRsLPKGIMVLL 413
Cdd:cd11038  238 MLTFAEHPDQWRALRE--DPELAPAA----------------VEEVLRWCPTTTWATREAVEDVEYNGVT-IPAGTVVHL 298
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158937242 414 SIYGLHHNPKVWPnPEVFDPFRFAPgsaqhshAFLPFSGGSRNCIGKQFAMNELkvATALTLLRfELLPDPTR 486
Cdd:cd11038  299 CSHAANRDPRVFD-ADRFDITAKRA-------PHLGFGGGVHHCLGAFLARAEL--AEALTVLA-RRLPTPAI 360
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
332-489 8.88e-13

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


Pssm-ID: 410725  Cd Length: 438  Bit Score: 70.02  E-value: 8.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 332 WILYALATHPKHQERCREEIHSLLGDGA---------SITWNHLDQMPYTTMCIKEALRL--YPPVPGIGRELSTpVTFP 400
Cdd:cd20632  237 WAMYYLLRHPEALAAVRDEIDHVLQSTGqelgpdfdiHLTREQLDSLVYLESAINESLRLssASMNIRVVQEDFT-LKLE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 401 DGRS--LPKGIMVLLSIYGLHHNPKVWPNPEV--FDPF--------RFAPGSAQHSHAFLPFSGGSRNCIGKQFAMNELK 468
Cdd:cd20632  316 SDGSvnLRKGDIVALYPQSLHMDPEIYEDPEVfkFDRFvedgkkktTFYKRGQKLKYYLMPFGSGSSKCPGRFFAVNEIK 395
                        170       180
                 ....*....|....*....|.
gi 158937242 469 VATALTLLRFELLPDPTRIPI 489
Cdd:cd20632  396 QFLSLLLLYFDLELLEEQKPP 416
PLN03234 PLN03234
cytochrome P450 83B1; Provisional
291-479 9.73e-13

cytochrome P450 83B1; Provisional


Pssm-ID: 178773 [Multi-domain]  Cd Length: 499  Bit Score: 70.49  E-value: 9.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 291 FLDILL-LAKMENGSI-LSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGDGASITWNHLDQ 368
Cdd:PLN03234 267 FIDLLMqIYKDQPFSIkFTHENVKAMILDIVVPGTDTAAAVVVWAMTYLIKYPEAMKKAQDEVRNVIGDKGYVSEEDIPN 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 369 MPYTTMCIKEALRLYPPVPGIGRELSTPVTFPDGRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFA---PGSAQHS 444
Cdd:PLN03234 347 LPYLKAVIKESLRLEPVIPILLHRETIADAKIGGYDIPAKTIIQVNAWAVSRDTAAWgDNPNEFIPERFMkehKGVDFKG 426
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 158937242 445 HAF--LPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:PLN03234 427 QDFelLPFGSGRRMCPAMHLGIAMVEIPFANLLYKFD 463
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
290-470 1.03e-12

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: 69.54  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 290 DFLDILLLAKMEnGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREeihsllgDGASItwnhldqm 369
Cdd:cd11035  171 DLISAILNAEID-GRPLTDDELLGLCFLLFLAGLDTVASALGFIFRHLARHPEDRRRLRE-------DPELI-------- 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 370 pytTMCIKEALRLYPPVpGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsAQHSHafLP 449
Cdd:cd11035  235 ---PAAVEELLRRYPLV-NVARIVTRDVEF-HGVQLKAGDMVLLPLALANRDPREFPDPDTVDFDR-----KPNRH--LA 302
                        170       180
                 ....*....|....*....|.
gi 158937242 450 FSGGSRNCIGKQFAMNELKVA 470
Cdd:cd11035  303 FGAGPHRCLGSHLARLELRIA 323
P450_EryK-like cd11032
cytochrome P450 EryK and similar cytochrome P450s; This subfamily contains archaeal and ...
284-479 1.27e-12

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


Pssm-ID: 410658 [Multi-domain]  Cd Length: 368  Bit Score: 69.17  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 284 KRKRHL--DFLDILLLAKMENGSiLSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLGdgasi 361
Cdd:cd11032  171 ERRRNPrdDLISRLVEAEVDGER-LTDEEIVGFAILLLIAGHETTTNLLGNAVLCLDEDPEVAARLRADPSLIPG----- 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 362 twnhldqmpyttmCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapGSA 441
Cdd:cd11032  245 -------------AIEEVLRYRPPVQRTARVTTEDVEL-GGVTIPAGQLVIAWLASANRDERQFEDPDTFDIDR---NPN 307
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 158937242 442 QHshafLPFSGGSRNCIGKQFAMNELKVATALTLLRFE 479
Cdd:cd11032  308 PH----LSFGHGIHFCLGAPLARLEARIALEALLDRFP 341
CYP142-like cd11033
cytochrome P450 family 142 and similar cytochrome P450s; This family is composed of cytochrome ...
293-488 2.29e-11

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: 65.24  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 293 DIL-LLAKME-NGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPkhqercrEEIHSLLGDGAsitwnHLDQMp 370
Cdd:cd11033  190 DLIsVLANAEvDGEPLTDEEFASFFILLAVAGNETTRNSISGGVLALAEHP-------DQWERLRADPS-----LLPTA- 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 371 yttmcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfAPGsaQHshafLPF 450
Cdd:cd11033  257 -----VEEILRWASPVIHFRRTATRDTEL-GGQRIRAGDKVVLWYASANRDEEVFDDPDRFDITR-SPN--PH----LAF 323
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 158937242 451 SGGSRNCIGKQFAMNELKVATA--LTLL-RFELLPDPTRIP 488
Cdd:cd11033  324 GGGPHFCLGAHLARLELRVLFEelLDRVpDIELAGEPERLR 364
PLN02500 PLN02500
cytochrome P450 90B1
304-478 3.57e-11

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 65.27  E-value: 3.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 304 SILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREE------IHSLLGDgASITWNHLDQMPYTTMCIK 377
Cdd:PLN02500 273 SNLSTEQILDLILSLLFAGHETSSVAIALAIFFLQGCPKAVQELREEhleiarAKKQSGE-SELNWEDYKKMEFTQCVIN 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 378 EALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRF-----APGSAQHSHA----FL 448
Cdd:PLN02500 352 ETLRLGNVVRFLHRKALKDVRY-KGYDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWqqnnnRGGSSGSSSAttnnFM 430
                        170       180       190
                 ....*....|....*....|....*....|
gi 158937242 449 PFSGGSRNCIGKQFAMNELKVATALTLLRF 478
Cdd:PLN02500 431 PFGGGPRLCAGSELAKLEMAVFIHHLVLNF 460
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
231-491 4.88e-11

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: 64.71  E-value: 4.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 231 RVRNA---FHQNDTIYSLTSAGRWTHrACQLAHQHTDQVIQ-LRKAQLQK-EGELEKIKRKRHLDfldilllakmENGSI 305
Cdd:cd20631  154 LILNAlenFKEFDKVFPALVAGLPIH-MFKTAKSAREALAErLLHENLQKrENISELISLRMLLN----------DTLST 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 306 LSDKDL-RAEVDTfMFEGHDTTASGISWILYALATHPKHQERCREEIHSLLG--------DGASITWN--HLDQMPYTTM 374
Cdd:cd20631  223 LDEMEKaRTHVAM-LWASQANTLPATFWSLFYLLRCPEAMKAATKEVKRTLEktgqkvsdGGNPIVLTreQLDDMPVLGS 301
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 375 CIKEALRLYPPVPGIGRELS-TPVTFPDGRSLP--KGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSAQHS------- 444
Cdd:cd20631  302 IIKEALRLSSASLNIRVAKEdFTLHLDSGESYAirKDDIIALYPQLLHLDPEIYEDPLTFKYDRYLDENGKEKttfykng 381
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 158937242 445 ----HAFLPFSGGSRNCIGKQFAMNELKVATALTLLRFEL-LPDPTRIPIPI 491
Cdd:cd20631  382 rklkYYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYFDMeLLDGNAKCPPL 433
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
333-481 2.40e-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: 62.66  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 333 ILYALATHPKH-QERCREEIHSLLGDGASITWNHLDQMPYTTMCIKEALRLYPPVP---GIGRELSTpVTFPDGR-SLPK 407
Cdd:cd11071  248 LLARLGLAGEElHARLAEEIRSALGSEGGLTLAALEKMPLLKSVVYETLRLHPPVPlqyGRARKDFV-IESHDASyKIKK 326
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 408 GIMVLLSIYGLHHNPKVWPNPEVFDPFRF-APGSAQHSHAFlpFSGG---------SRNCIGKQFAMNELKVATALTLLR 477
Cdd:cd11071  327 GELLVGYQPLATRDPKVFDNPDEFVPDRFmGEEGKLLKHLI--WSNGpeteeptpdNKQCPGKDLVVLLARLFVAELFLR 404

                 ....
gi 158937242 478 FELL 481
Cdd:cd11071  405 YDTF 408
CYP_Pc22g25500-like cd20626
cytochrome P450 Pc22g25500 and similar cytochrome P450s; Penicillium rubens Pc22g25500 is a ...
376-460 3.55e-10

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: 61.65  E-value: 3.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 376 IKEALRLYPPVPGIGRelstpvTFPDgRSLPKGIMVLLSIYGLHHNPKVW-PNPEVFDPFRFAPGSAQHSHAFLPFSGGS 454
Cdd:cd20626  262 VKEALRLYPPTRRIYR------AFQR-PGSSKPEIIAADIEACHRSESIWgPDALEFNPSRWSKLTPTQKEAFLPFGSGP 334

                 ....*.
gi 158937242 455 RNCIGK 460
Cdd:cd20626  335 FRCPAK 340
PLN03141 PLN03141
3-epi-6-deoxocathasterone 23-monooxygenase; Provisional
265-463 1.14e-09

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


Pssm-ID: 215600 [Multi-domain]  Cd Length: 452  Bit Score: 60.52  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 265 QVIQLRKAQLQKEGELEKIKRKrhlDFLDILLlakMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQ 344
Cdd:PLN03141 212 KIIEEKRRAMKNKEEDETGIPK---DVVDVLL---RDGSDELTDDLISDNMIDMMIPGEDSVPVLMTLAVKFLSDCPVAL 285
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 345 ERCREE---IHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHH 420
Cdd:PLN03141 286 QQLTEEnmkLKRLKADtGEPLYWTDYMSLPFTQNVITETLRMGNIINGVMRKAMKDVEI-KGYLIPKGWCVLAYFRSVHL 364
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 158937242 421 NPKVWPNPEVFDPFRFAPGSAQHShAFLPFSGGSRNCIGKQFA 463
Cdd:PLN03141 365 DEENYDNPYQFNPWRWQEKDMNNS-SFTPFGGGQRLCPGLDLA 406
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
378-508 1.41e-09

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: 59.66  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 378 EALRLYPPVPGIGRELSTPVTFPDG----RSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfaPgsaqhSHAFLPFSGG 453
Cdd:cd20612  246 EALRLNPIAPGLYRRATTDTTVADGggrtVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR--P-----LESYIHFGHG 318
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 158937242 454 SRNCIGKQFAMnelKVATALtLLRFELLPDPTRIPIPIARLVLKSKNGIHLRLRR 508
Cdd:cd20612  319 PHQCLGEEIAR---AALTEM-LRVVLRLPNLRRAPGPQGELKKIPRGGFKAYLRE 369
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
278-488 1.67e-09

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: 60.07  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 278 GELEKIKRKRHLdFLDILLLAKM---ENGS-ILSDKD-LRAEV-------DTFMF----EGHDTTASGISWILYALATHP 341
Cdd:cd20633  177 KDKLEAERLKRL-FWDMLSVSKMsqkENISgWISEQQrQLAEHgmpeymqDRFMFlllwASQGNTGPASFWLLLYLLKHP 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 342 KHQERCREEIHSLL----------GDGASITWNHLDQMPYTTMCIKEALRLyPPVPGIGRELSTPVTF--PDGR--SLPK 407
Cdd:cd20633  256 EAMKAVREEVEQVLketgqevkpgGPLINLTRDMLLKTPVLDSAVEETLRL-TAAPVLIRAVVQDMTLkmANGReyALRK 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 408 GIMVLLSIY-GLHHNPKVWPNPEVFDPFRFAPGSAQHSHAF-----------LPFSGGSRNCIGKQFAMNELK--VATAL 473
Cdd:cd20633  335 GDRLALFPYlAVQMDPEIHPEPHTFKYDRFLNPDGGKKKDFykngkklkyynMPWGAGVSICPGRFFAVNEMKqfVFLML 414
                        250
                 ....*....|....*
gi 158937242 474 TLLRFELLPDPTRIP 488
Cdd:cd20633  415 TYFDLELVNPDEEIP 429
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
295-470 6.90e-09

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: 57.75  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 295 LLLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEihsllgdgasitwnhLDQMPyttM 374
Cdd:cd11079  168 RLLRERVDGRPLTDEEIVSILRNWTVGELGTIAACVGVLVHYLARHPELQARLRAN---------------PALLP---A 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 375 CIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapgsaqHSHAFLPFSGGS 454
Cdd:cd11079  230 AIDEILRLDDPFVANRRITTRDVEL-GGRTIPAGSRVTLNWASANRDERVFGDPDEFDPDR-------HAADNLVYGRGI 301
                        170
                 ....*....|....*.
gi 158937242 455 RNCIGKQFAMNELKVA 470
Cdd:cd11079  302 HVCPGAPLARLELRIL 317
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
332-488 1.28e-08

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


Pssm-ID: 410727 [Multi-domain]  Cd Length: 442  Bit Score: 57.08  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 332 WILYALATHPKHQERCREEIHSLLGDGASITWNH-------LDQMPYTTMCIKEALRLyPPVPGIGRELSTPVTFP--DG 402
Cdd:cd20634  243 WLLLFLLKHPEAMAAVRGEIQRIKHQRGQPVSQTltinqelLDNTPVFDSVLSETLRL-TAAPFITREVLQDMKLRlaDG 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 403 R--SLPKGIMVLLSIY-GLHHNPKVWPNPEVFDPFRF--APGS---------AQHSHAFLPFSGGSRNCIGKQFAMNELK 468
Cdd:cd20634  322 QeyNLRRGDRLCLFPFlSPQMDPEIHQEPEVFKYDRFlnADGTekkdfykngKRLKYYNMPWGAGDNVCIGRHFAVNSIK 401
                        170       180
                 ....*....|....*....|..
gi 158937242 469 --VATALTLLRFELLPDPTRIP 488
Cdd:cd20634  402 qfVFLILTHFDVELKDPEAEIP 423
CYP105-like cd11030
cytochrome P450 family 105 and similar cytochrome P450s; This group predominantly contains ...
293-510 2.33e-08

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: 55.99  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 293 DIL--LLAKMENGSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERCREEIHslLGDGAsitwnhldqmp 370
Cdd:cd11030  189 DLLsrLVAEHGAPGELTDEELVGIAVLLLVAGHETTANMIALGTLALLEHPEQLAALRADPS--LVPGA----------- 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 371 yttmcIKEALRLYPPVP-GIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapGSAQHshafLP 449
Cdd:cd11030  256 -----VEELLRYLSIVQdGLPRVATEDVEI-GGVTIRAGEGVIVSLPAANRDPAVFPDPDRLDITR---PARRH----LA 322
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 158937242 450 FSGGSRNCIGKQFAMNELKVA-TALtLLRFellpdPT-RIPIPIARLVLKSKNGIHlRLRRLP 510
Cdd:cd11030  323 FGHGVHQCLGQNLARLELEIAlPTL-FRRF-----PGlRLAVPAEELPFRPDSLVY-GVHELP 378
AknT-like cd11036
AknT-like proteins; This family is composed of proteins similar to Streptomyces biosynthesis ...
363-486 5.09e-05

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: 45.56  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 363 WNHLDQMPYT-TMCIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRFAPGSA 441
Cdd:cd11036  211 WARLRPDPELaAAAVAETLRYDPPVRLERRFAAEDLEL-AGVTLPAGDHVVVLLAAANRDPEAFPDPDRFDLGRPTARSA 289
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 158937242 442 qhshaflPFSGGSRNCIGKQFAMneLKVATALTLLRfELLPDPTR 486
Cdd:cd11036  290 -------HFGLGRHACLGAALAR--AAAAAALRALA-ARFPGLRA 324
PLN02648 PLN02648
allene oxide synthase
330-436 7.29e-05

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 45.31  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 330 ISWIlyALAThPKHQERCREEIHSLLGD-GASITWNHLDQMPYTTMCIKEALRLYPPVPgigrelstpvtFPDGRslPKG 408
Cdd:PLN02648 296 LKWV--GRAG-EELQARLAEEVRSAVKAgGGGVTFAALEKMPLVKSVVYEALRIEPPVP-----------FQYGR--ARE 359
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 158937242 409 IMVLLS------------IYGLH----HNPKVWPNPEVFDPFRF 436
Cdd:PLN02648 360 DFVIEShdaafeikkgemLFGYQplvtRDPKVFDRPEEFVPDRF 403
P450-pinF2-like cd11039
P450-pinF2 and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) ...
296-484 1.27e-04

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


Pssm-ID: 410665 [Multi-domain]  Cd Length: 372  Bit Score: 44.42  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 296 LLAKMEN-GSILSDKDLRAEVDTFMFEGHDTTASGISWILYALATHPKHQERC-REEIHSLLGdgasitwnhldqmpytt 373
Cdd:cd11039  187 LLSVMLNaGMPMSLEQIRANIKVAIGGGLNEPRDAIAGTCWGLLSNPEQLAEVmAGDVHWLRA----------------- 249
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158937242 374 mcIKEALRLYPPVPGIGRELSTPVTFpDGRSLPKGIMVLLSIYGLHHNPKVWPNPEVFDPFRfapGSAQHshafLPFSGG 453
Cdd:cd11039  250 --FEEGLRWISPIGMSPRRVAEDFEI-RGVTLPAGDRVFLMFGSANRDEARFENPDRFDVFR---PKSPH----VSFGAG 319
                        170       180       190
                 ....*....|....*....|....*....|....
gi 158937242 454 SRNCIGKQFA---MNELKVATALTLLRFELLPDP 484
Cdd:cd11039  320 PHFCAGAWASrqmVGEIALPELFRRLPNLIRLDP 353
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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