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Conserved domains on  [gi|1834010771|gb|KAF4194141|]
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hypothetical protein CNMCM8694_007916 [Aspergillus lentulus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00911 super family cl00340
dihydroxy-acid dehydratase; Provisional
1336-1918 0e+00

dihydroxy-acid dehydratase; Provisional


The actual alignment was detected with superfamily member PRK06131:

Pssm-ID: 469730  Cd Length: 571  Bit Score: 825.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1336 GLRQGLTSYGDAHFSLFLRKVFIKALGYSEDALS-RPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTIS 1414
Cdd:PRK06131     3 GLLRSLAWFGDDDFRAFYHRSFMKNQGYPDELFDgRPIIGICNTWSDLNPCNAHFRQLAERVKRGVLEAGGFPVEFPVIS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1415 IHESFSHPTSMFLRNLMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTD 1494
Cdd:PRK06131    83 LGESFLRPTAMLYRNLAAMDVEEMIRGYPIDGVVLLGGCDKTTPALLMGAASVDLPAIVLSGGPMLNGKHKGERLGSGTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1495 CRNNWAAFRAGDIDIEEISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAA 1574
Cdd:PRK06131   163 VWKYWEELRAGEIDLEEFLEAEAGMARSAGTCNTMGTASTMACMAEALGMSLPGNAAIPAVDARRIRMAELTGRRIVEMV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1575 LAKRRPQDILSKESFLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFH 1653
Cdd:PRK06131   243 HEDLKPSDILTREAFENAIRVNAAIGGSTNAVIHLIAIAGR----AGVeLDLDDWDRIGRDVPVLVNLQPSGEYLMEDFY 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1654 NAGGMLALLHTLRPLLHFSAMTISGQTLGEVLDASPfrtfPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASK 1733
Cdd:PRK06131   319 YAGGLPAVLRELGELLHLDALTVNGKTLGENLAGAP----VYNDDVIRPLDNPLKPEGGIAVLRGNLAPDGAVIKPSAAS 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1734 DrRLVSHTGPAVVFESPEDLAKRIDDPDLDVTKDSVLVLKGIGPIGNPGMPEAGLIPIPRKLASAGVKDMLRLSDGRMSG 1813
Cdd:PRK06131   395 P-ELLKHEGRAVVFEGYEDYKARIDDPDLDVDEDTVLVLRNAGPKGYPGMPEVGNMPIPKKLLRQGVKDMVRISDARMSG 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1814 TAGGTIVLHISPESALpESPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEgsdlakgwlDRTRRRGYRSLYE 1893
Cdd:PRK06131   474 TAYGTVVLHVAPEAAA-GGPLALVRTGDRIRLDVPARRLDLLVSDEELARRRAAWPPP---------PPRAERGYQELYR 543
                          570       580
                   ....*....|....*....|....*
gi 1834010771 1894 RSVNQAPDGADFDFLTAVGPSDVSK 1918
Cdd:PRK06131   544 DHVLQADEGCDFDFLVGYRGAPVPR 568
RNA12 pfam10443
RNA12 protein; This family includes RNA12 from S. cerevisiae. That protein contains an RRM ...
366-784 0e+00

RNA12 protein; This family includes RNA12 from S. cerevisiae. That protein contains an RRM domain. This region is C-terminal to that and includes a P-loop motif suggesting this region binds to NTP. The RNA12 proteins is involved in pre-rRNA maturation.


:

Pssm-ID: 371055  Cd Length: 429  Bit Score: 731.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  366 RQEDITRLQSWLMENVETFIVVHGPRGSGKRELVLDRALVDYKYKLVLDCKQIQDARGDSAKIARAASQVGYRPVFSWMN 445
Cdd:pfam10443    1 RKEKIEQLQEWLLENVNTFIVVQGPRGSGKRELVMDRVLKDRKNVLVIDCDQLQKARGDAGFISTAASQVGYFPVFSWMN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  446 SISSFIDLAAQGMIGTKAGFSETLDAQLSNIWQNTATALKKVTLEHRKKNDKDSHLTDEEYLEAHPELRPVVVIDNYLHN 525
Cdd:pfam10443   81 SISSLIDLAAQGLTGQKAGFSETKEAQLRNILQTTATALKDIALEEYKKEDKDANLKEEDYLEAHPEAKPVVVIDNFLHK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  526 ASESSVVYDKITEWAAGLTAGNIAHVIFLTTDVSYAKPLSKALPNSVFRTITLGDCSLEVGRKFVVNHLAYE-------S 598
Cdd:pfam10443  161 AEENGFVYKKLAEWAASLVQNNIAHVIFLTEDVSYSKPLSKALPNQVFKTISLGDASPDVARKYVLSQLDEDtrkeensS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  599 KDGKTQPGRA----EELEDLDACIETLGGRVTDLEFMAHRIEAGETPRGAVNRIIEQSASEILKMFLLT-PETIEQSWTH 673
Cdd:pfam10443  241 DEQNTDDKAAtaneKDLKELDSCIEPLGGRMTDLQAFARRIKSGESPSEAVNDIIEQSASEILKMFLLDsGDASDLPWTP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  674 EQAWYLIKRLaeSKDGALSYNEIVLSELFKENGEITLRALEHAELISITAVNGCPQTIRPGKPVLRAAFKKVTENKALSS 753
Cdd:pfam10443  321 EQAWYLIKLL--SKNGSIPYNELLLSPLFKGSGETALRALEQAELISVTRDNGRPSTIRPGKPVYRAAFKRLLNDKVLSS 398
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1834010771  754 RMDLAIIAQKVNKENKSIGKYEEELSLLGSL 784
Cdd:pfam10443  399 RLDLEYLTALIAKENKKIKKYEEELRLLGKL 429
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
828-1313 4.66e-94

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: 311.99  E-value: 4.66e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  828 FVRRARDYMDEA-VFGIILGGSKHDVVVSPSLTKAILASRGTSSTALI-NYTLEKIWGDKGAIRnlsATDHHIIHHNIPN 905
Cdd:cd11040      1 LLRNGKKYFSGGpIFTIRLGGQKIYVITDPELISAVFRNPKTLSFDPIvIVVVGRVFGSPESAK---KKEGEPGGKGLIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  906 LLMR--EPFLTEaSKAAKDITERETPNLvtfcRSMVDQAPWErrseaevidgKEKPTAEVNLFALVRNFVGHISTSVSMG 983
Cdd:cd11040     78 LLHDlhKKALSG-GEGLDRLNEAMLENL----SKLLDELSLS----------GGTSTVEVDLYEWLRDVLTRATTEALFG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  984 QAFLEAFPNLLDDMWDFDNRFLAMSFGAPRWLplpgLSAAYAARDRILDAFAAYHQAfvswdegndpGVKFRDldDVSEP 1063
Cdd:cd11040    143 PKLPELDPDLVEDFWTFDRGLPKLLLGLPRLL----ARKAYAARDRLLKALEKYYQA----------AREERD--DGSEL 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1064 MKQRIRKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFanahrpsreetgLPFQEPA 1143
Cdd:cd11040    207 IRARAKVLREAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPA------------VTPDSGT 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1144 KISLDPDELFRSCPLLKASFYETMRLDSAGLSFREVTSDLTvtespedaaaanlgDPRTYRIKKGGNIIMAHGVVQRDPQ 1223
Cdd:cd11040    275 NAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTV--------------LGGGYLLRKGSLVMIPPRLLHMDPE 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1224 LF-SNPEQFDPLRFIVTDPDTGAQKaDMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEFAIPGHRPS 1302
Cdd:cd11040    341 IWgPDPEEFDPERFLKKDGDKKGRG-LPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMDES 419
                          490
                   ....*....|...
gi 1834010771 1303 --SGAYLPKNDIK 1313
Cdd:cd11040    420 pgLGILPPKRDVR 432
RRM_SF super family cl17169
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
181-279 3.72e-28

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


The actual alignment was detected with superfamily member cd12433:

Pssm-ID: 473069 [Multi-domain]  Cd Length: 86  Bit Score: 109.28  E-value: 3.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  181 RIPSPRLKVAFHPvsPEASaadlnTETLYTLFRPYGKIRDIEKQPSDSKvtPRYAFVEFSRPKYAGMAKNCMHGFTVPEq 260
Cdd:cd12433      1 RYPSRTIRVEFEG--PELS-----QEELYSLFRPYGRINDITPPPPDSL--PRYATVTFRRIRGAIAAKNCLHGYVVNE- 70
                           90
                   ....*....|....*....
gi 1834010771  261 egggkSGTRLKIKYERKIK 279
Cdd:cd12433     71 -----GGTRLRIQYEPKLR 84
 
Name Accession Description Interval E-value
PRK06131 PRK06131
dihydroxy-acid dehydratase; Validated
1336-1918 0e+00

dihydroxy-acid dehydratase; Validated


Pssm-ID: 235708  Cd Length: 571  Bit Score: 825.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1336 GLRQGLTSYGDAHFSLFLRKVFIKALGYSEDALS-RPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTIS 1414
Cdd:PRK06131     3 GLLRSLAWFGDDDFRAFYHRSFMKNQGYPDELFDgRPIIGICNTWSDLNPCNAHFRQLAERVKRGVLEAGGFPVEFPVIS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1415 IHESFSHPTSMFLRNLMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTD 1494
Cdd:PRK06131    83 LGESFLRPTAMLYRNLAAMDVEEMIRGYPIDGVVLLGGCDKTTPALLMGAASVDLPAIVLSGGPMLNGKHKGERLGSGTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1495 CRNNWAAFRAGDIDIEEISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAA 1574
Cdd:PRK06131   163 VWKYWEELRAGEIDLEEFLEAEAGMARSAGTCNTMGTASTMACMAEALGMSLPGNAAIPAVDARRIRMAELTGRRIVEMV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1575 LAKRRPQDILSKESFLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFH 1653
Cdd:PRK06131   243 HEDLKPSDILTREAFENAIRVNAAIGGSTNAVIHLIAIAGR----AGVeLDLDDWDRIGRDVPVLVNLQPSGEYLMEDFY 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1654 NAGGMLALLHTLRPLLHFSAMTISGQTLGEVLDASPfrtfPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASK 1733
Cdd:PRK06131   319 YAGGLPAVLRELGELLHLDALTVNGKTLGENLAGAP----VYNDDVIRPLDNPLKPEGGIAVLRGNLAPDGAVIKPSAAS 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1734 DrRLVSHTGPAVVFESPEDLAKRIDDPDLDVTKDSVLVLKGIGPIGNPGMPEAGLIPIPRKLASAGVKDMLRLSDGRMSG 1813
Cdd:PRK06131   395 P-ELLKHEGRAVVFEGYEDYKARIDDPDLDVDEDTVLVLRNAGPKGYPGMPEVGNMPIPKKLLRQGVKDMVRISDARMSG 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1814 TAGGTIVLHISPESALpESPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEgsdlakgwlDRTRRRGYRSLYE 1893
Cdd:PRK06131   474 TAYGTVVLHVAPEAAA-GGPLALVRTGDRIRLDVPARRLDLLVSDEELARRRAAWPPP---------PPRAERGYQELYR 543
                          570       580
                   ....*....|....*....|....*
gi 1834010771 1894 RSVNQAPDGADFDFLTAVGPSDVSK 1918
Cdd:PRK06131   544 DHVLQADEGCDFDFLVGYRGAPVPR 568
RNA12 pfam10443
RNA12 protein; This family includes RNA12 from S. cerevisiae. That protein contains an RRM ...
366-784 0e+00

RNA12 protein; This family includes RNA12 from S. cerevisiae. That protein contains an RRM domain. This region is C-terminal to that and includes a P-loop motif suggesting this region binds to NTP. The RNA12 proteins is involved in pre-rRNA maturation.


Pssm-ID: 371055  Cd Length: 429  Bit Score: 731.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  366 RQEDITRLQSWLMENVETFIVVHGPRGSGKRELVLDRALVDYKYKLVLDCKQIQDARGDSAKIARAASQVGYRPVFSWMN 445
Cdd:pfam10443    1 RKEKIEQLQEWLLENVNTFIVVQGPRGSGKRELVMDRVLKDRKNVLVIDCDQLQKARGDAGFISTAASQVGYFPVFSWMN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  446 SISSFIDLAAQGMIGTKAGFSETLDAQLSNIWQNTATALKKVTLEHRKKNDKDSHLTDEEYLEAHPELRPVVVIDNYLHN 525
Cdd:pfam10443   81 SISSLIDLAAQGLTGQKAGFSETKEAQLRNILQTTATALKDIALEEYKKEDKDANLKEEDYLEAHPEAKPVVVIDNFLHK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  526 ASESSVVYDKITEWAAGLTAGNIAHVIFLTTDVSYAKPLSKALPNSVFRTITLGDCSLEVGRKFVVNHLAYE-------S 598
Cdd:pfam10443  161 AEENGFVYKKLAEWAASLVQNNIAHVIFLTEDVSYSKPLSKALPNQVFKTISLGDASPDVARKYVLSQLDEDtrkeensS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  599 KDGKTQPGRA----EELEDLDACIETLGGRVTDLEFMAHRIEAGETPRGAVNRIIEQSASEILKMFLLT-PETIEQSWTH 673
Cdd:pfam10443  241 DEQNTDDKAAtaneKDLKELDSCIEPLGGRMTDLQAFARRIKSGESPSEAVNDIIEQSASEILKMFLLDsGDASDLPWTP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  674 EQAWYLIKRLaeSKDGALSYNEIVLSELFKENGEITLRALEHAELISITAVNGCPQTIRPGKPVLRAAFKKVTENKALSS 753
Cdd:pfam10443  321 EQAWYLIKLL--SKNGSIPYNELLLSPLFKGSGETALRALEQAELISVTRDNGRPSTIRPGKPVYRAAFKRLLNDKVLSS 398
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1834010771  754 RMDLAIIAQKVNKENKSIGKYEEELSLLGSL 784
Cdd:pfam10443  399 RLDLEYLTALIAKENKKIKKYEEELRLLGKL 429
ILVD_EDD pfam00920
Dehydratase family;
1370-1903 0e+00

Dehydratase family;


Pssm-ID: 459998  Cd Length: 513  Bit Score: 676.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1370 RPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI------HESFSHpTSMFLRNLMSMDTEEMIRAQP 1443
Cdd:pfam00920    1 KPIIGIANSYSDLVPCHVHLRELAEAVKEGVREAGGVPAEFNTIGVcdgiamGHEGMR-YSLPSRELIADSIEEMLRAHP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1444 LDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGshrgqriGACTDCRNNWAAFRAGDIDIEEISAINDELAPTI 1523
Cdd:pfam00920   80 FDGLVLIGGCDKIVPGMLMAAARLNIPAIFVSGGPMLPG-------GSGTDEFEAVGAYAAGKISEEELLEIERAACPGC 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1524 GTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKRRPQDILSKESFLNAITVLQAIGGST 1603
Cdd:pfam00920  153 GSCGGMGTANTMACLAEALGLSLPGSATIPAVSAERLRLAREAGRRIVELVEEDIKPRDILTRKAFENAIVVDMALGGST 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1604 NAVVHLMAIVNRHpklqGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTLRP-LLHFSAMTISGQTL 1681
Cdd:pfam00920  233 NAVLHLLAIAREA----GVdLTLDDFDRISRKVPLLADLKPSGKYLMEDFHRAGGVPAVLKELLDaLLHGDVLTVTGKTL 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1682 GEVLDASPFRtfpfSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDRRLVsHTGPAVVFESPEDLAKRIDDPd 1761
Cdd:pfam00920  309 GENLADAEVR----DQDVIRPLDNPISPTGGLAVLKGNLAPDGAVVKTSAVDPEMLV-FEGPARVFDSEEDALAAILDG- 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1762 lDVTKDSVLVLKGIGPIGNPGMPEagLIPIPRKLASAGV-KDMLRLSDGRMSGTAGGTIVLHISPESALpESPFGVVQTG 1840
Cdd:pfam00920  383 -KIKAGDVVVIRYEGPKGGPGMPE--MLTPTSALLGAGLgKDVALITDGRFSGASRGPSIGHVSPEAAV-GGPIALVRDG 458
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834010771 1841 DMITCDADHGKLTLEISDEELKSRIQTRKKEGSdlakgwldRTRRRGYRSLYERSVNQAPDGA 1903
Cdd:pfam00920  459 DIIRIDIPNRTLDLLVSDEELAARRAAWKPPEP--------KVKGRGYLAKYAKLVSSASEGA 513
IlvD COG0129
Dihydroxyacid dehydratase/phosphogluconate dehydratase [Amino acid transport and metabolism, ...
1359-1903 8.74e-151

Dihydroxyacid dehydratase/phosphogluconate dehydratase [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; Dihydroxyacid dehydratase/phosphogluconate dehydratase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439899  Cd Length: 558  Bit Score: 477.19  E-value: 8.74e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1359 KALGYSEDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI-------HE--SFSHPTsmflRN 1429
Cdd:COG0129     23 RATGLTDEDFGKPIIGIANSWNEIVPGHVHLDDLAEAVKEGIRAAGGVPFEFNTIAVsdgiamgHEgmRYSLPS----RE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1430 LMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLpLVT-GPMMPGSHRGQRIGAcTDCRNNWAAFRAGDID 1508
Cdd:COG0129     99 LIADSIETMVNAHCFDGLVCIPGCDKITPGMLMAAARLNIPSI-FVYgGPMLPGKYDGKDLDI-VDVFEAVGAYAAGKIS 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1509 IEEISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKRRPQDILSKES 1588
Cdd:COG0129    177 DEELKEIERNACPGCGSCSGMFTANTMACLTEALGLSLPGSGTIPAVSAERRRLAREAGRRIVELVEKDIKPRDILTREA 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1589 FLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTL-- 1665
Cdd:COG0129    257 FENAIAVDMALGGSTNTVLHLLAIAHE----AGVdLTLDDFDRISRRTPHLCDLKPSGKYHMEDLHRAGGIPAVMKELld 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1666 RPLLHFSAMTISGQTLGEVLDASPfrtFPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDRRLVsHTGPAV 1745
Cdd:COG0129    333 AGLLHGDCLTVTGKTLAENLADAD---IDRDQDVIRPLDNPYSPTGGLAILRGNLAPDGAVVKTAGVDESMLV-FEGPAR 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1746 VFESPEDLAKRIDDPdlDVTKDSVLVLKGIGPIGNPGMPEAgLIPIPrKLASAG-VKDMLRLSDGRMSGTAGGTIVLHIS 1824
Cdd:COG0129    409 VFDSEEEAVEAILGG--KIKAGDVVVIRYEGPKGGPGMREM-LSPTS-ALKGMGlGKSVALITDGRFSGGTRGLSIGHVS 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1825 PESAlpE-SPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEGSDLAKGWLDRtrrrgyrslYERSVNQAPDGA 1903
Cdd:COG0129    485 PEAA--EgGPIALVEDGDIITIDIPARTLDLLVSDEELARRRAAWKPPEPRVTSGVLAK---------YAKLVSSASKGA 553
ilvD TIGR00110
dihydroxy-acid dehydratase; This protein, dihydroxy-acid dehydratase, catalyzes the fourth ...
1360-1903 1.10e-125

dihydroxy-acid dehydratase; This protein, dihydroxy-acid dehydratase, catalyzes the fourth step in valine and isoleucine biosynthesis. It contains a catalytically essential [4Fe-4S] cluster This model generates scores of up to 150 bits vs. 6-phosphogluconate dehydratase, a homologous enzyme. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272910  Cd Length: 535  Bit Score: 406.42  E-value: 1.10e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1360 ALGYSEDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI-------HES--FSHPTsmflRNL 1430
Cdd:TIGR00110    1 ATGFTDEDFGKPFIGVANSYTTIVPGHMHLRDLAQAVKEGIEAAGGVAFEFNTIAVcdgiamgHEGmkYSLPS----REI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1431 MSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTDCRNNWAAFRAGDIDIE 1510
Cdd:TIGR00110   77 IADSVETMVNAHRFDGLVCIPSCDKITPGMLMAAARLNIPSIFVTGGPMLPGHTKLGKKIDLVSAFEAVGEYAAGKISEE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1511 EISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKRRPQDILSKESFL 1590
Cdd:TIGR00110  157 ELEEIERSACPGCGSCSGMFTANTMACLTEALGLSLPGCSTMLATSAEKKRIAKNSGKRIVELVKKNIKPRDILTKEAFE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1591 NAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTL--RP 1667
Cdd:TIGR00110  237 NAITVDMALGGSTNTVLHLLAIANE----AGVdLSLDDFDRLSRKVPHIASLAPSGKYVMEDLHRAGGIPAVLKELdrEG 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1668 LLHFSAMTISGQTLGEVLDASPFRtfPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDRRLVsHTGPAVVF 1747
Cdd:TIGR00110  313 LLHGDTLTVTGKTLGEILEQAPVI--PEGQDVIRPLDNPVHQEGGLAILKGNLAPNGAVVKIAGVDEDMTK-FEGPAKVF 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1748 ESPEDLAKRIDDPdlDVTKDSVLVLKGIGPIGNPGMPEAgLIPIPrKLASAGV-KDMLRLSDGRMSGTAGGTIVLHISPE 1826
Cdd:TIGR00110  390 ESEEEALEAILGG--KIKEGDVVVIRYEGPKGGPGMPEM-LAPTS-AIKGMGLgKSVALITDGRFSGGTRGLCIGHVSPE 465
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1827 SALpESPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEGSDLAKGWLDRtrrrgYRSLyersVNQAPDGA 1903
Cdd:TIGR00110  466 AAE-GGPIALVEDGDIIIIDIPNRKLDLQVSDEELAERRASWKAPEPRYVKGYLAK-----YAKL----VSSADEGA 532
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
828-1313 4.66e-94

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: 311.99  E-value: 4.66e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  828 FVRRARDYMDEA-VFGIILGGSKHDVVVSPSLTKAILASRGTSSTALI-NYTLEKIWGDKGAIRnlsATDHHIIHHNIPN 905
Cdd:cd11040      1 LLRNGKKYFSGGpIFTIRLGGQKIYVITDPELISAVFRNPKTLSFDPIvIVVVGRVFGSPESAK---KKEGEPGGKGLIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  906 LLMR--EPFLTEaSKAAKDITERETPNLvtfcRSMVDQAPWErrseaevidgKEKPTAEVNLFALVRNFVGHISTSVSMG 983
Cdd:cd11040     78 LLHDlhKKALSG-GEGLDRLNEAMLENL----SKLLDELSLS----------GGTSTVEVDLYEWLRDVLTRATTEALFG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  984 QAFLEAFPNLLDDMWDFDNRFLAMSFGAPRWLplpgLSAAYAARDRILDAFAAYHQAfvswdegndpGVKFRDldDVSEP 1063
Cdd:cd11040    143 PKLPELDPDLVEDFWTFDRGLPKLLLGLPRLL----ARKAYAARDRLLKALEKYYQA----------AREERD--DGSEL 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1064 MKQRIRKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFanahrpsreetgLPFQEPA 1143
Cdd:cd11040    207 IRARAKVLREAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPA------------VTPDSGT 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1144 KISLDPDELFRSCPLLKASFYETMRLDSAGLSFREVTSDLTvtespedaaaanlgDPRTYRIKKGGNIIMAHGVVQRDPQ 1223
Cdd:cd11040    275 NAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTV--------------LGGGYLLRKGSLVMIPPRLLHMDPE 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1224 LF-SNPEQFDPLRFIVTDPDTGAQKaDMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEFAIPGHRPS 1302
Cdd:cd11040    341 IWgPDPEEFDPERFLKKDGDKKGRG-LPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMDES 419
                          490
                   ....*....|...
gi 1834010771 1303 --SGAYLPKNDIK 1313
Cdd:cd11040    420 pgLGILPPKRDVR 432
RRM_Yme2p_like cd12433
RNA recognition motif (RRM) found in yeast mitochondrial escape protein 2 (Yme2p) and similar ...
181-279 3.72e-28

RNA recognition motif (RRM) found in yeast mitochondrial escape protein 2 (Yme2p) and similar proteins; This subfamily corresponds to the RRM of Yme2p, also termed protein RNA12, an inner mitochondrial membrane protein that plays a critical role in mitochondrial DNA transactions. It may serve as a mediator of nucleoid structure and number in mitochondria of the yeast Saccharomyces cerevisiae. Yme2p contains an exonuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal domain.


Pssm-ID: 409867 [Multi-domain]  Cd Length: 86  Bit Score: 109.28  E-value: 3.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  181 RIPSPRLKVAFHPvsPEASaadlnTETLYTLFRPYGKIRDIEKQPSDSKvtPRYAFVEFSRPKYAGMAKNCMHGFTVPEq 260
Cdd:cd12433      1 RYPSRTIRVEFEG--PELS-----QEELYSLFRPYGRINDITPPPPDSL--PRYATVTFRRIRGAIAAKNCLHGYVVNE- 70
                           90
                   ....*....|....*....
gi 1834010771  261 egggkSGTRLKIKYERKIK 279
Cdd:cd12433     71 -----GGTRLRIQYEPKLR 84
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
825-1293 6.75e-22

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: 101.20  E-value: 6.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  825 HINFVRRARDYmdEAVFGIILGGSKHDVVVSPSLTKAILASRGTSSTALIN----YTLEKIWGDKGAIRNLSATdhhiiH 900
Cdd:pfam00067   23 HSVFTKLQKKY--GPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDepwfATSRGPFLGKGIVFANGPR-----W 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  901 HNIPNLLMREpFLTEASKAAKDITERETPNLVTFCRSMVDQAPwerrseaeVIDgkekPTAEVNLFALvrNFVGHISTSV 980
Cdd:pfam00067   96 RQLRRFLTPT-FTSFGKLSFEPRVEEEARDLVEKLRKTAGEPG--------VID----ITDLLFRAAL--NVICSILFGE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  981 SMGQAFLEAFPNLLDDMWDfdnRFLAMSFGAPR-WLPLPGL----SAAYAARDRILDAFAAYHQAFV-----SWDEGNDP 1050
Cdd:pfam00067  161 RFGSLEDPKFLELVKAVQE---LSSLLSSPSPQlLDLFPILkyfpGPHGRKLKRARKKIKDLLDKLIeerreTLDSAKKS 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1051 GVKFRDLddvsepMKQRIRKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIapfanahrp 1130
Cdd:pfam00067  238 PRDFLDA------LLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEI--------- 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1131 sreETGLPFQEPAKISlDPDELfrscPLLKASFYETMRL-DSAGLS-FREVTSDLTVtespedaaaanlgdpRTYRIKKG 1208
Cdd:pfam00067  303 ---DEVIGDKRSPTYD-DLQNM----PYLDAVIKETLRLhPVVPLLlPREVTKDTVI---------------PGYLIPKG 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1209 GNIIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDTGAQKadmHTIY--PFGGGVSGCKGRALAERTILLFSAAIISMWDI 1286
Cdd:pfam00067  360 TLVIVNLYALHRDPEVFPNPEEFDPERF---LDENGKFR---KSFAflPFGAGPRNCLGERLARMEMKLFLATLLQNFEV 433

                   ....*..
gi 1834010771 1287 EPASGKE 1293
Cdd:pfam00067  434 ELPPGTD 440
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
1157-1309 2.24e-10

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: 64.91  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDS-AGLSFREVTSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLR 1235
Cdd:COG2124    268 ELLPAAVEETLRLYPpVPLLPRTATEDVE------------LGG---VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR 332
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834010771 1236 fivtdpdtgaqkaDMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMW-DIEPASGKEfaiPGHRPSSGAYLPK 1309
Cdd:COG2124    333 -------------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFpDLRLAPPEE---LRWRPSLTLRGPK 391
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1075-1297 2.68e-08

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 58.41  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1075 GLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFAnahRPSREETGLPFQEPAKIsldpdelfr 1154
Cdd:PLN02196   259 GLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIR---KDKEEGESLTWEDTKKM--------- 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1155 scPLLKASFYETMRLDSAgLSFrevtsdlTVTESPEDAaaanlgDPRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPL 1234
Cdd:PLN02196   327 --PLTSRVIQETLRVASI-LSF-------TFREAVEDV------EYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPS 390
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834010771 1235 RFIVtdpdtgAQKADmhTIYPFGGGVSGCKGRALA--ERTILLFSAAIISMWDI-EPASGKE---FAIP 1297
Cdd:PLN02196   391 RFEV------APKPN--TFMPFGNGTHSCPGNELAklEISVLIHHLTTKYRWSIvGTSNGIQygpFALP 451
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
202-258 1.62e-07

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 49.92  E-value: 1.62e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771  202 DLNTETLYTLFRPYGKIRDIEKQPSDSKVTPRYAFVEFSRPKYAGMAKNCMHGFTVP 258
Cdd:pfam00076    9 DTTEEDLKDLFSKFGPIKSIRLVRDETGRSKGFAFVEFEDEEDAEKAIEALNGKELG 65
RRM smart00360
RNA recognition motif;
202-257 1.70e-05

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.51  E-value: 1.70e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771   202 DLNTETLYTLFRPYGKIRDIE-KQPSDSKVTPRYAFVEFSRPKYAGMAKNCMHGFTV 257
Cdd:smart00360   10 DTTEEELRELFSKFGKVESVRlVRDKETGKSKGFAFVEFESEEDAEKALEALNGKEL 66
 
Name Accession Description Interval E-value
PRK06131 PRK06131
dihydroxy-acid dehydratase; Validated
1336-1918 0e+00

dihydroxy-acid dehydratase; Validated


Pssm-ID: 235708  Cd Length: 571  Bit Score: 825.20  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1336 GLRQGLTSYGDAHFSLFLRKVFIKALGYSEDALS-RPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTIS 1414
Cdd:PRK06131     3 GLLRSLAWFGDDDFRAFYHRSFMKNQGYPDELFDgRPIIGICNTWSDLNPCNAHFRQLAERVKRGVLEAGGFPVEFPVIS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1415 IHESFSHPTSMFLRNLMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTD 1494
Cdd:PRK06131    83 LGESFLRPTAMLYRNLAAMDVEEMIRGYPIDGVVLLGGCDKTTPALLMGAASVDLPAIVLSGGPMLNGKHKGERLGSGTD 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1495 CRNNWAAFRAGDIDIEEISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAA 1574
Cdd:PRK06131   163 VWKYWEELRAGEIDLEEFLEAEAGMARSAGTCNTMGTASTMACMAEALGMSLPGNAAIPAVDARRIRMAELTGRRIVEMV 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1575 LAKRRPQDILSKESFLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFH 1653
Cdd:PRK06131   243 HEDLKPSDILTREAFENAIRVNAAIGGSTNAVIHLIAIAGR----AGVeLDLDDWDRIGRDVPVLVNLQPSGEYLMEDFY 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1654 NAGGMLALLHTLRPLLHFSAMTISGQTLGEVLDASPfrtfPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASK 1733
Cdd:PRK06131   319 YAGGLPAVLRELGELLHLDALTVNGKTLGENLAGAP----VYNDDVIRPLDNPLKPEGGIAVLRGNLAPDGAVIKPSAAS 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1734 DrRLVSHTGPAVVFESPEDLAKRIDDPDLDVTKDSVLVLKGIGPIGNPGMPEAGLIPIPRKLASAGVKDMLRLSDGRMSG 1813
Cdd:PRK06131   395 P-ELLKHEGRAVVFEGYEDYKARIDDPDLDVDEDTVLVLRNAGPKGYPGMPEVGNMPIPKKLLRQGVKDMVRISDARMSG 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1814 TAGGTIVLHISPESALpESPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEgsdlakgwlDRTRRRGYRSLYE 1893
Cdd:PRK06131   474 TAYGTVVLHVAPEAAA-GGPLALVRTGDRIRLDVPARRLDLLVSDEELARRRAAWPPP---------PPRAERGYQELYR 543
                          570       580
                   ....*....|....*....|....*
gi 1834010771 1894 RSVNQAPDGADFDFLTAVGPSDVSK 1918
Cdd:PRK06131   544 DHVLQADEGCDFDFLVGYRGAPVPR 568
RNA12 pfam10443
RNA12 protein; This family includes RNA12 from S. cerevisiae. That protein contains an RRM ...
366-784 0e+00

RNA12 protein; This family includes RNA12 from S. cerevisiae. That protein contains an RRM domain. This region is C-terminal to that and includes a P-loop motif suggesting this region binds to NTP. The RNA12 proteins is involved in pre-rRNA maturation.


Pssm-ID: 371055  Cd Length: 429  Bit Score: 731.80  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  366 RQEDITRLQSWLMENVETFIVVHGPRGSGKRELVLDRALVDYKYKLVLDCKQIQDARGDSAKIARAASQVGYRPVFSWMN 445
Cdd:pfam10443    1 RKEKIEQLQEWLLENVNTFIVVQGPRGSGKRELVMDRVLKDRKNVLVIDCDQLQKARGDAGFISTAASQVGYFPVFSWMN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  446 SISSFIDLAAQGMIGTKAGFSETLDAQLSNIWQNTATALKKVTLEHRKKNDKDSHLTDEEYLEAHPELRPVVVIDNYLHN 525
Cdd:pfam10443   81 SISSLIDLAAQGLTGQKAGFSETKEAQLRNILQTTATALKDIALEEYKKEDKDANLKEEDYLEAHPEAKPVVVIDNFLHK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  526 ASESSVVYDKITEWAAGLTAGNIAHVIFLTTDVSYAKPLSKALPNSVFRTITLGDCSLEVGRKFVVNHLAYE-------S 598
Cdd:pfam10443  161 AEENGFVYKKLAEWAASLVQNNIAHVIFLTEDVSYSKPLSKALPNQVFKTISLGDASPDVARKYVLSQLDEDtrkeensS 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  599 KDGKTQPGRA----EELEDLDACIETLGGRVTDLEFMAHRIEAGETPRGAVNRIIEQSASEILKMFLLT-PETIEQSWTH 673
Cdd:pfam10443  241 DEQNTDDKAAtaneKDLKELDSCIEPLGGRMTDLQAFARRIKSGESPSEAVNDIIEQSASEILKMFLLDsGDASDLPWTP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  674 EQAWYLIKRLaeSKDGALSYNEIVLSELFKENGEITLRALEHAELISITAVNGCPQTIRPGKPVLRAAFKKVTENKALSS 753
Cdd:pfam10443  321 EQAWYLIKLL--SKNGSIPYNELLLSPLFKGSGETALRALEQAELISVTRDNGRPSTIRPGKPVYRAAFKRLLNDKVLSS 398
                          410       420       430
                   ....*....|....*....|....*....|.
gi 1834010771  754 RMDLAIIAQKVNKENKSIGKYEEELSLLGSL 784
Cdd:pfam10443  399 RLDLEYLTALIAKENKKIKKYEEELRLLGKL 429
ILVD_EDD pfam00920
Dehydratase family;
1370-1903 0e+00

Dehydratase family;


Pssm-ID: 459998  Cd Length: 513  Bit Score: 676.74  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1370 RPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI------HESFSHpTSMFLRNLMSMDTEEMIRAQP 1443
Cdd:pfam00920    1 KPIIGIANSYSDLVPCHVHLRELAEAVKEGVREAGGVPAEFNTIGVcdgiamGHEGMR-YSLPSRELIADSIEEMLRAHP 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1444 LDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGshrgqriGACTDCRNNWAAFRAGDIDIEEISAINDELAPTI 1523
Cdd:pfam00920   80 FDGLVLIGGCDKIVPGMLMAAARLNIPAIFVSGGPMLPG-------GSGTDEFEAVGAYAAGKISEEELLEIERAACPGC 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1524 GTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKRRPQDILSKESFLNAITVLQAIGGST 1603
Cdd:pfam00920  153 GSCGGMGTANTMACLAEALGLSLPGSATIPAVSAERLRLAREAGRRIVELVEEDIKPRDILTRKAFENAIVVDMALGGST 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1604 NAVVHLMAIVNRHpklqGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTLRP-LLHFSAMTISGQTL 1681
Cdd:pfam00920  233 NAVLHLLAIAREA----GVdLTLDDFDRISRKVPLLADLKPSGKYLMEDFHRAGGVPAVLKELLDaLLHGDVLTVTGKTL 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1682 GEVLDASPFRtfpfSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDRRLVsHTGPAVVFESPEDLAKRIDDPd 1761
Cdd:pfam00920  309 GENLADAEVR----DQDVIRPLDNPISPTGGLAVLKGNLAPDGAVVKTSAVDPEMLV-FEGPARVFDSEEDALAAILDG- 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1762 lDVTKDSVLVLKGIGPIGNPGMPEagLIPIPRKLASAGV-KDMLRLSDGRMSGTAGGTIVLHISPESALpESPFGVVQTG 1840
Cdd:pfam00920  383 -KIKAGDVVVIRYEGPKGGPGMPE--MLTPTSALLGAGLgKDVALITDGRFSGASRGPSIGHVSPEAAV-GGPIALVRDG 458
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1834010771 1841 DMITCDADHGKLTLEISDEELKSRIQTRKKEGSdlakgwldRTRRRGYRSLYERSVNQAPDGA 1903
Cdd:pfam00920  459 DIIRIDIPNRTLDLLVSDEELAARRAAWKPPEP--------KVKGRGYLAKYAKLVSSASEGA 513
PRK13016 PRK13016
dihydroxy-acid dehydratase; Provisional
1361-1914 0e+00

dihydroxy-acid dehydratase; Provisional


Pssm-ID: 237271  Cd Length: 577  Bit Score: 592.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1361 LGYS-EDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISIHESFSHPTSMFLRNLMSMDTEEMI 1439
Cdd:PRK13016    32 MGYApEDFDGKPVIAILNTWSDANPCHGHFRERVEDVKRGVLQAGGFPLELPALSLSENFVKPTTMLYRNLLAMETEELI 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1440 RAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTDCRNNWAAFRAGDIDIEEISAINDEL 1519
Cdd:PRK13016   112 RSHPVDGAVLMGGCDKTTPGLVMGAISMGLPMIYLPAGPMLRGNYRGKVLGSGSDAWKYWDERRAGNITQAEWLEIEGGI 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1520 APTIGTCGVMGTASTMACITAALGLMpLRGASA-PAVSSARVRIAEETGAHAVAAALAKRRPQDILSKESFLNAITVLQA 1598
Cdd:PRK13016   192 ARSYGTCMTMGTASTMTAIAEALGLT-LPGASSiPAADANHQRMAALCGRRIVEMVWEDLTPSQILTKAAFENAITVAMA 270
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1599 IGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNY-MNDFHNAGGMLALLHTLRPLLHFSAMTI 1676
Cdd:PRK13016   271 TGCSTNAVIHLIAMARR----AGVpLSLDDLDRCGRTVPVIANIRPSGKTYlMEDFFYAGGLRALMKQLGDKLHLDALTV 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1677 SGQTLGEVLDASPFrtfpFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASkDRRLVSHTGPAVVFESPEDLAKR 1756
Cdd:PRK13016   347 TGKTLGDNLEGAKV----YNDDVIRPLDNPVYAEGSLAVLRGNLAPDGAVIKPAAC-DPKFLVHRGPALVFDSYPEMKAA 421
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1757 IDDPDLDVTKDSVLVLKGIGPIGNPGMPEAGLIPIPRKLASAGVKDMLRLSDGRMSGTAGGTIVLHISPESALpESPFGV 1836
Cdd:PRK13016   422 IDDENLDVTPDHVMVLRNAGPQGGPGMPEWGMLPIPKKLLKQGVRDMVRISDARMSGTSYGACVLHVAPEAYV-GGPLAL 500
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1837 VQTGDMITCDADHGKLTLEISDEELKSRIqtrkkegsdlaKGWLDRTRR--RGYRSLYERSVNQAPDGADFDFL-TAVGP 1913
Cdd:PRK13016   501 VRTGDIIELDVPARRLHLLVSDEELARRR-----------AAWQPPERRyeRGYGWMFSQHVEQADKGCDFDFLeTGFGR 569

                   .
gi 1834010771 1914 S 1914
Cdd:PRK13016   570 A 570
PRK13017 PRK13017
dihydroxy-acid dehydratase; Provisional
1370-1909 2.73e-167

dihydroxy-acid dehydratase; Provisional


Pssm-ID: 237272  Cd Length: 596  Bit Score: 523.37  E-value: 2.73e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1370 RPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISIHESFSHPTSMFLRNLMSMDTEEMIRAQPLDACIM 1449
Cdd:PRK13017    47 KPIIGIAQTGSDLSPCNRHHLELAERVKEGIRDAGGIPMEFPVHPIQETGKRPTAALDRNLAYLGLVEILYGYPLDGVVL 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1450 IGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTDCRNNWAAFRAGDIDIEEISAINDELAPTIGTCGVM 1529
Cdd:PRK13017   127 TTGCDKTTPACLMAAATVDLPAIVLSGGPMLDGWHEGERVGSGTVIWKARELLAAGEIDYEEFMELVASSAPSVGHCNTM 206
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1530 GTASTMACITAALGlMPLRGASA-PAVSSARVRIAEETGAHAVAAALAKRRPQDILSKESFLNAITVLQAIGGSTNAVVH 1608
Cdd:PRK13017   207 GTASTMNALAEALG-MSLPGCAAiPAPYRERGQMAYATGKRIVEMVWEDLKPSDILTREAFENAIVVNSAIGGSTNAPIH 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1609 LMAIVnRHpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTLRP--LLHFSAMTISGQTLGEVL 1685
Cdd:PRK13017   286 LIAIA-RH---AGVeLSLDDWQRVGEDVPLLVNLQPAGKYLGEDFHRAGGVPAVLAELLRagLLHGDALTVSGRTIGENI 361
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1686 DASPfrtfPFSQQVIRPLSNPLYPSSSLVVLRGNIApDGAIIKASA----------SKDRRLVSHTGPAVVFESPEDLAK 1755
Cdd:PRK13017   362 AGAP----APDRDVIRPYDAPLKERAGFLVLRGNLF-DSAIMKTSViseefrerylSEPGDENAFEGRAVVFDGPEDYHA 436
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1756 RIDDPDLDVTKDSVLVLKGIGPIGNPGMPEAGLIPIPRKLASAGVKDMLRLSDGRMSGTAGGTIVLHISPESALpESPFG 1835
Cdd:PRK13017   437 RIDDPALDIDEHCILVIRGAGPVGYPGSAEVVNMQPPAALLKRGIRSLPCIGDGRQSGTSGSPSILNASPEAAV-GGGLA 515
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834010771 1836 VVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEGSDLAKGWldrtrrrgyRSLYERSVNQAPDGADFDFLT 1909
Cdd:PRK13017   516 LLRTGDRIRIDLNKRRVDVLVSDEELARRRAALKPPVPPSQTPW---------QELYRKHVGQLSTGACLEPAT 580
IlvD COG0129
Dihydroxyacid dehydratase/phosphogluconate dehydratase [Amino acid transport and metabolism, ...
1359-1903 8.74e-151

Dihydroxyacid dehydratase/phosphogluconate dehydratase [Amino acid transport and metabolism, Carbohydrate transport and metabolism]; Dihydroxyacid dehydratase/phosphogluconate dehydratase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis


Pssm-ID: 439899  Cd Length: 558  Bit Score: 477.19  E-value: 8.74e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1359 KALGYSEDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI-------HE--SFSHPTsmflRN 1429
Cdd:COG0129     23 RATGLTDEDFGKPIIGIANSWNEIVPGHVHLDDLAEAVKEGIRAAGGVPFEFNTIAVsdgiamgHEgmRYSLPS----RE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1430 LMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLpLVT-GPMMPGSHRGQRIGAcTDCRNNWAAFRAGDID 1508
Cdd:COG0129     99 LIADSIETMVNAHCFDGLVCIPGCDKITPGMLMAAARLNIPSI-FVYgGPMLPGKYDGKDLDI-VDVFEAVGAYAAGKIS 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1509 IEEISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKRRPQDILSKES 1588
Cdd:COG0129    177 DEELKEIERNACPGCGSCSGMFTANTMACLTEALGLSLPGSGTIPAVSAERRRLAREAGRRIVELVEKDIKPRDILTREA 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1589 FLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTL-- 1665
Cdd:COG0129    257 FENAIAVDMALGGSTNTVLHLLAIAHE----AGVdLTLDDFDRISRRTPHLCDLKPSGKYHMEDLHRAGGIPAVMKELld 332
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1666 RPLLHFSAMTISGQTLGEVLDASPfrtFPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDRRLVsHTGPAV 1745
Cdd:COG0129    333 AGLLHGDCLTVTGKTLAENLADAD---IDRDQDVIRPLDNPYSPTGGLAILRGNLAPDGAVVKTAGVDESMLV-FEGPAR 408
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1746 VFESPEDLAKRIDDPdlDVTKDSVLVLKGIGPIGNPGMPEAgLIPIPrKLASAG-VKDMLRLSDGRMSGTAGGTIVLHIS 1824
Cdd:COG0129    409 VFDSEEEAVEAILGG--KIKAGDVVVIRYEGPKGGPGMREM-LSPTS-ALKGMGlGKSVALITDGRFSGGTRGLSIGHVS 484
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1825 PESAlpE-SPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEGSDLAKGWLDRtrrrgyrslYERSVNQAPDGA 1903
Cdd:COG0129    485 PEAA--EgGPIALVEDGDIITIDIPARTLDLLVSDEELARRRAAWKPPEPRVTSGVLAK---------YAKLVSSASKGA 553
PRK00911 PRK00911
dihydroxy-acid dehydratase; Provisional
1357-1903 2.94e-144

dihydroxy-acid dehydratase; Provisional


Pssm-ID: 234861  Cd Length: 552  Bit Score: 458.76  E-value: 2.94e-144
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1357 FIKALGYSEDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI-------HE--SFSHPTsmfl 1427
Cdd:PRK00911    18 MLRATGLTDEDFDKPFIGIANSWNEITPCNIHLNELADAVKEGVRAAGGVPFEFNTIGVsdgiamgHEgmKYSLVS---- 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1428 RNLMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRI---------GACTdcrnn 1498
Cdd:PRK00911    94 REVIADSIETVVNAHWFDGLVAIPGCDKNMPGMLMAAARLNVPSIFVYGGPILPGRLKGKDLtlvsvfeavGAYA----- 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1499 waafrAGDIDIEEISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKR 1578
Cdd:PRK00911   169 -----AGKISEEELKEIERNACPGAGSCGGMFTANTMACLIEALGMSLPGSGTIPAVDAERDELAREAGEAVVELLEKDI 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1579 RPQDILSKESFLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGG 1657
Cdd:PRK00911   244 KPRDILTREAFENAIAVDMALGGSTNAVLHLLAIAHE----AGVdLTLDDFNRISKRTPHLADLKPSGKYVMEDLHEAGG 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1658 MLALLHTL--RPLLHFSAMTISGQTLGEVLDASPfrtfPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDR 1735
Cdd:PRK00911   320 IPAVMKELldAGLLHGDCLTVTGKTLAENLADAP----DPDQDVIRPLDNPISPTGGLAILKGNLAPEGAVVKIAGVKPE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1736 RlvsHTGPAVVFESPEDLAKRIDDPdlDVTKDSVLVLKGIGPIGNPGMPE----------AGLIpiprklasagvKDMLR 1805
Cdd:PRK00911   396 M---FTGPARVFDSEEEAMEAILAG--KIKAGDVVVIRYEGPKGGPGMREmlaptsaivgAGLG-----------DDVAL 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1806 LSDGRMSGTAGGTIVLHISPESAlpES-PFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEGSDLAKGWLDRtr 1884
Cdd:PRK00911   460 ITDGRFSGGTRGLCVGHVSPEAA--VGgPIALVEDGDIITIDAPNRTLDVLVSDEELARRRAAWKPPEPKYKRGVLAK-- 535
                          570
                   ....*....|....*....
gi 1834010771 1885 rrgyrslYERSVNQAPDGA 1903
Cdd:PRK00911   536 -------YAKLVSSASTGA 547
ilvD TIGR00110
dihydroxy-acid dehydratase; This protein, dihydroxy-acid dehydratase, catalyzes the fourth ...
1360-1903 1.10e-125

dihydroxy-acid dehydratase; This protein, dihydroxy-acid dehydratase, catalyzes the fourth step in valine and isoleucine biosynthesis. It contains a catalytically essential [4Fe-4S] cluster This model generates scores of up to 150 bits vs. 6-phosphogluconate dehydratase, a homologous enzyme. [Amino acid biosynthesis, Pyruvate family]


Pssm-ID: 272910  Cd Length: 535  Bit Score: 406.42  E-value: 1.10e-125
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1360 ALGYSEDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI-------HES--FSHPTsmflRNL 1430
Cdd:TIGR00110    1 ATGFTDEDFGKPFIGVANSYTTIVPGHMHLRDLAQAVKEGIEAAGGVAFEFNTIAVcdgiamgHEGmkYSLPS----REI 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1431 MSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTDCRNNWAAFRAGDIDIE 1510
Cdd:TIGR00110   77 IADSVETMVNAHRFDGLVCIPSCDKITPGMLMAAARLNIPSIFVTGGPMLPGHTKLGKKIDLVSAFEAVGEYAAGKISEE 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1511 EISAINDELAPTIGTCGVMGTASTMACITAALGLMPLRGASAPAVSSARVRIAEETGAHAVAAALAKRRPQDILSKESFL 1590
Cdd:TIGR00110  157 ELEEIERSACPGCGSCSGMFTANTMACLTEALGLSLPGCSTMLATSAEKKRIAKNSGKRIVELVKKNIKPRDILTKEAFE 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1591 NAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNYMNDFHNAGGMLALLHTL--RP 1667
Cdd:TIGR00110  237 NAITVDMALGGSTNTVLHLLAIANE----AGVdLSLDDFDRLSRKVPHIASLAPSGKYVMEDLHRAGGIPAVLKELdrEG 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1668 LLHFSAMTISGQTLGEVLDASPFRtfPFSQQVIRPLSNPLYPSSSLVVLRGNIAPDGAIIKASASKDRRLVsHTGPAVVF 1747
Cdd:TIGR00110  313 LLHGDTLTVTGKTLGEILEQAPVI--PEGQDVIRPLDNPVHQEGGLAILKGNLAPNGAVVKIAGVDEDMTK-FEGPAKVF 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1748 ESPEDLAKRIDDPdlDVTKDSVLVLKGIGPIGNPGMPEAgLIPIPrKLASAGV-KDMLRLSDGRMSGTAGGTIVLHISPE 1826
Cdd:TIGR00110  390 ESEEEALEAILGG--KIKEGDVVVIRYEGPKGGPGMPEM-LAPTS-AIKGMGLgKSVALITDGRFSGGTRGLCIGHVSPE 465
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1827 SALpESPFGVVQTGDMITCDADHGKLTLEISDEELKSRIQTRKKEGSDLAKGWLDRtrrrgYRSLyersVNQAPDGA 1903
Cdd:TIGR00110  466 AAE-GGPIALVEDGDIIIIDIPNRKLDLQVSDEELAERRASWKAPEPRYVKGYLAK-----YAKL----VSSADEGA 532
CYP7_CYP8-like cd11040
cytochrome P450s similar to cytochrome P450 family 7, subfamily A, polypeptide 1, cytochrome ...
828-1313 4.66e-94

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: 311.99  E-value: 4.66e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  828 FVRRARDYMDEA-VFGIILGGSKHDVVVSPSLTKAILASRGTSSTALI-NYTLEKIWGDKGAIRnlsATDHHIIHHNIPN 905
Cdd:cd11040      1 LLRNGKKYFSGGpIFTIRLGGQKIYVITDPELISAVFRNPKTLSFDPIvIVVVGRVFGSPESAK---KKEGEPGGKGLIR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  906 LLMR--EPFLTEaSKAAKDITERETPNLvtfcRSMVDQAPWErrseaevidgKEKPTAEVNLFALVRNFVGHISTSVSMG 983
Cdd:cd11040     78 LLHDlhKKALSG-GEGLDRLNEAMLENL----SKLLDELSLS----------GGTSTVEVDLYEWLRDVLTRATTEALFG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  984 QAFLEAFPNLLDDMWDFDNRFLAMSFGAPRWLplpgLSAAYAARDRILDAFAAYHQAfvswdegndpGVKFRDldDVSEP 1063
Cdd:cd11040    143 PKLPELDPDLVEDFWTFDRGLPKLLLGLPRLL----ARKAYAARDRLLKALEKYYQA----------AREERD--DGSEL 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1064 MKQRIRKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFanahrpsreetgLPFQEPA 1143
Cdd:cd11040    207 IRARAKVLREAGLSEEDIARAELALLWAINANTIPAAFWLLAHILSDPELLERIREEIEPA------------VTPDSGT 274
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1144 KISLDPDELFRSCPLLKASFYETMRLDSAGLSFREVTSDLTvtespedaaaanlgDPRTYRIKKGGNIIMAHGVVQRDPQ 1223
Cdd:cd11040    275 NAILDLTDLLTSCPLLDSTYLETLRLHSSSTSVRLVTEDTV--------------LGGGYLLRKGSLVMIPPRLLHMDPE 340
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1224 LF-SNPEQFDPLRFIVTDPDTGAQKaDMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEFAIPGHRPS 1302
Cdd:cd11040    341 IWgPDPEEFDPERFLKKDGDKKGRG-LPGAFRPFGGGASLCPGRHFAKNEILAFVALLLSRFDVEPVGGGDWKVPGMDES 419
                          490
                   ....*....|...
gi 1834010771 1303 --SGAYLPKNDIK 1313
Cdd:cd11040    420 pgLGILPPKRDVR 432
PRK12448 PRK12448
dihydroxy-acid dehydratase; Provisional
1359-1886 9.56e-68

dihydroxy-acid dehydratase; Provisional


Pssm-ID: 237104  Cd Length: 615  Bit Score: 241.67  E-value: 9.56e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1359 KALGYSEDALSRPIIGIINTFSGFNPCHANVPQLIEAVKRGIQLNGGLAIEFPTISI-------HES--FSHPTsmflRN 1429
Cdd:PRK12448    22 RATGMKDEDFGKPIIAVVNSFTQFVPGHVHLKDLGQLVAREIEAAGGVAKEFNTIAVddgiamgHGGmlYSLPS----RE 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1430 LMSMDTEEMIRAQPLDACIMIGGCDKTVPAQLMGGISANKPVLPLVTGPMMPGSHRGQRIGACTDCRNnwAAFRAGD--I 1507
Cdd:PRK12448    98 LIADSVEYMVNAHCADAMVCISNCDKITPGMLMAALRLNIPVVFVSGGPMEAGKTKLSDKIIKLDLVD--AMVAAADpsV 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1508 DIEEISAINDELAPTIGTCGVMGTASTMACITAALGL-MPLRGaSAPAVSSARVRIAEETGAHAVAAAlakRR------- 1579
Cdd:PRK12448   176 SDEDVAQIERSACPTCGSCSGMFTANSMNCLTEALGLsLPGNG-SLLATHADRKQLFLEAGRRIVELA---KRyyeqdde 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1580 ---PQDILSKESFLNAITVLQAIGGSTNAVVHLMAIVNRhpklQGV-ITLDTFAEIGRRTPLLIDLKPSGDNY-MNDFHN 1654
Cdd:PRK12448   252 svlPRSIATKAAFENAMTLDIAMGGSTNTVLHLLAAAQE----AEVdFTMADIDRLSRKVPCLCKVAPNTQKYhMEDVHR 327
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1655 AGGMLALLHTLRP--LLHFSAMTISGQTLGEVLD-----------------ASP---FRTFPFSQQ-------------V 1699
Cdd:PRK12448   328 AGGIMGILGELDRagLLHTDVPTVHGLTLGEALDqwdimrtqdeavkeffrAAPggiRTTVAFSQDcrwdsldtdrengC 407
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1700 IRPLSNPLYPSSSLVVLRGNIAPDGAIIKaSASKDRRLVSHTGPAVVFESPED-----LAKRIDDPDldvtkdsVLVLKG 1774
Cdd:PRK12448   408 IRSVEHAYSKDGGLAVLYGNIAEDGCIVK-TAGVDESILKFTGPARVFESQDDaveaiLGGKVKAGD-------VVVIRY 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1775 IGPIGNPGMPEAgLIPIPRkLASAGV-KDMLRLSDGRMSGTAGGTIVLHISPESAlPESPFGVVQTGDMITCDADHGKLT 1853
Cdd:PRK12448   480 EGPKGGPGMQEM-LYPTSY-LKSKGLgKACALITDGRFSGGTSGLSIGHVSPEAA-SGGAIGLVEDGDIIEIDIPNRSIN 556
                          570       580       590
                   ....*....|....*....|....*....|...
gi 1834010771 1854 LEISDEELKSRiqtRKKEGSDLAKGWLDRTRRR 1886
Cdd:PRK12448   557 LLVSDEELAAR---RAAQEARGDKAWKPKNRER 586
RRM_Yme2p_like cd12433
RNA recognition motif (RRM) found in yeast mitochondrial escape protein 2 (Yme2p) and similar ...
181-279 3.72e-28

RNA recognition motif (RRM) found in yeast mitochondrial escape protein 2 (Yme2p) and similar proteins; This subfamily corresponds to the RRM of Yme2p, also termed protein RNA12, an inner mitochondrial membrane protein that plays a critical role in mitochondrial DNA transactions. It may serve as a mediator of nucleoid structure and number in mitochondria of the yeast Saccharomyces cerevisiae. Yme2p contains an exonuclease domain, an RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal domain.


Pssm-ID: 409867 [Multi-domain]  Cd Length: 86  Bit Score: 109.28  E-value: 3.72e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  181 RIPSPRLKVAFHPvsPEASaadlnTETLYTLFRPYGKIRDIEKQPSDSKvtPRYAFVEFSRPKYAGMAKNCMHGFTVPEq 260
Cdd:cd12433      1 RYPSRTIRVEFEG--PELS-----QEELYSLFRPYGRINDITPPPPDSL--PRYATVTFRRIRGAIAAKNCLHGYVVNE- 70
                           90
                   ....*....|....*....
gi 1834010771  261 egggkSGTRLKIKYERKIK 279
Cdd:cd12433     71 -----GGTRLRIQYEPKLR 84
CYP7A1 cd20631
cytochrome P450 family 7, subfamily A, polypeptide 1; Cytochrome P450 7A1 (CYP7A1) is also ...
989-1313 1.17e-25

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: 112.47  E-value: 1.17e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  989 AFPNLLDDMWDFDNRFLAMSFGaprwLPLPGLSAAYAARDRILDAFaaYHQafvswdegndpgvKFRDLDDVSEPMKQRI 1068
Cdd:cd20631    154 LILNALENFKEFDKVFPALVAG----LPIHMFKTAKSAREALAERL--LHE-------------NLQKRENISELISLRM 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1069 RKFKEL-GLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIapfanahRPSREETGlpfQEPA---- 1143
Cdd:cd20631    215 LLNDTLsTLDEMEKARTHVAMLWASQANTLPATFWSLFYLLRCPEAMKAATKEV-------KRTLEKTG---QKVSdggn 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1144 KISLDPDELfRSCPLLKASFYETMRLDSAGLSFREVTSDLTVTespedaaaanLGDPRTYRIKKGGNIIMAHGVVQRDPQ 1223
Cdd:cd20631    285 PIVLTREQL-DDMPVLGSIIKEALRLSSASLNIRVAKEDFTLH----------LDSGESYAIRKDDIIALYPQLLHLDPE 353
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1224 LFSNPEQFDPLRFIvtdPDTGAQKADM--------HTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIE--PASGKE 1293
Cdd:cd20631    354 IYEDPLTFKYDRYL---DENGKEKTTFykngrklkYYYMPFGSGTSKCPGRFFAINEIKQFLSLMLCYFDMEllDGNAKC 430
                          330       340
                   ....*....|....*....|
gi 1834010771 1294 FAIPGHRPSSGAYLPKNDIK 1313
Cdd:cd20631    431 PPLDQSRAGLGILPPTHDVD 450
cytochrome_P450 cd00302
cytochrome P450 (CYP) superfamily; Cytochrome P450 (P450, CYP) is a large superfamily of ...
852-1310 3.51e-23

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: 104.13  E-value: 3.51e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  852 VVVSPSLTKAILASRGTSSTALINYTLEKIWGDKGAIRNLSATDHHIIHHNIpnllmrEPFLTeaskaaKDITERETPNL 931
Cdd:cd00302     15 VVSDPELVREVLRDPRDFSSDAGPGLPALGDFLGDGLLTLDGPEHRRLRRLL------APAFT------PRALAALRPVI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  932 VTFCRSMVDQapWERRSEAEVidgkekptaevNLFALVRNFVGHISTSVSMGQAFLEAFPNLLDDMWDFdnrFLAMSFGA 1011
Cdd:cd00302     83 REIARELLDR--LAAGGEVGD-----------DVADLAQPLALDVIARLLGGPDLGEDLEELAELLEAL---LKLLGPRL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1012 PRWLPLPGLSAAYAARDRILDAFAAYHQAFvswdegndpgvkfRDLDDVSEPMKQRIRKFKELGLSPRSSAPGHLSLFWA 1091
Cdd:cd00302    147 LRPLPSPRLRRLRRARARLRDYLEELIARR-------------RAEPADDLDLLLLADADDGGGLSDEEIVAELLTLLLA 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1092 LNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRPsreetglpfqepakisldpdELFRSCPLLKASFYETMRLDS 1171
Cdd:cd00302    214 GHETTASLLAWALYLLARHPEVQERLRAEIDAVLGDGTP--------------------EDLSKLPYLEAVVEETLRLYP 273
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1172 -AGLSFREVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdpdtGAQKADM 1250
Cdd:cd00302    274 pVPLLPRVATEDVELGG---------------YTIPAGTLVLLSLYAAHRDPEVFPDPDEFDPERFL------PEREEPR 332
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1251 HTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEfaiPGHRPSSGAYLPKN 1310
Cdd:cd00302    333 YAHLPFGAGPHRCLGARLARLELKLALATLLRRFDFELVPDEE---LEWRPSLGTLGPAS 389
p450 pfam00067
Cytochrome P450; Cytochrome P450s are haem-thiolate proteins involved in the oxidative ...
825-1293 6.75e-22

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: 101.20  E-value: 6.75e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  825 HINFVRRARDYmdEAVFGIILGGSKHDVVVSPSLTKAILASRGTSSTALIN----YTLEKIWGDKGAIRNLSATdhhiiH 900
Cdd:pfam00067   23 HSVFTKLQKKY--GPIFRLYLGPKPVVVLSGPEAVKEVLIKKGEEFSGRPDepwfATSRGPFLGKGIVFANGPR-----W 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  901 HNIPNLLMREpFLTEASKAAKDITERETPNLVTFCRSMVDQAPwerrseaeVIDgkekPTAEVNLFALvrNFVGHISTSV 980
Cdd:pfam00067   96 RQLRRFLTPT-FTSFGKLSFEPRVEEEARDLVEKLRKTAGEPG--------VID----ITDLLFRAAL--NVICSILFGE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  981 SMGQAFLEAFPNLLDDMWDfdnRFLAMSFGAPR-WLPLPGL----SAAYAARDRILDAFAAYHQAFV-----SWDEGNDP 1050
Cdd:pfam00067  161 RFGSLEDPKFLELVKAVQE---LSSLLSSPSPQlLDLFPILkyfpGPHGRKLKRARKKIKDLLDKLIeerreTLDSAKKS 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1051 GVKFRDLddvsepMKQRIRKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIapfanahrp 1130
Cdd:pfam00067  238 PRDFLDA------LLLAKEEEDGSKLTDEELRATVLELFFAGTDTTSSTLSWALYELAKHPEVQEKLREEI--------- 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1131 sreETGLPFQEPAKISlDPDELfrscPLLKASFYETMRL-DSAGLS-FREVTSDLTVtespedaaaanlgdpRTYRIKKG 1208
Cdd:pfam00067  303 ---DEVIGDKRSPTYD-DLQNM----PYLDAVIKETLRLhPVVPLLlPREVTKDTVI---------------PGYLIPKG 359
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1209 GNIIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDTGAQKadmHTIY--PFGGGVSGCKGRALAERTILLFSAAIISMWDI 1286
Cdd:pfam00067  360 TLVIVNLYALHRDPEVFPNPEEFDPERF---LDENGKFR---KSFAflPFGAGPRNCLGERLARMEMKLFLATLLQNFEV 433

                   ....*..
gi 1834010771 1287 EPASGKE 1293
Cdd:pfam00067  434 ELPPGTD 440
Cyp8B1 cd20633
cytochrome P450 family 8, subfamily B, polypeptide 1; Cytochrome P450 8B1 (CYP8B1) is also ...
1058-1313 4.44e-16

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: 83.19  E-value: 4.44e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1058 DDVSEPMKQRIRKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIApfaNAHRPSREETGl 1137
Cdd:cd20633    202 ENISGWISEQQRQLAEHGMPEYMQDRFMFLLLWASQGNTGPASFWLLLYLLKHPEAMKAVREEVE---QVLKETGQEVK- 277
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1138 pfQEPAKISLDPDELFRScPLLKASFYETMRLDSAGLSFREVTSDLTVtespedaaaaNLGDPRTYRIKKGGNIIM-AHG 1216
Cdd:cd20633    278 --PGGPLINLTRDMLLKT-PVLDSAVEETLRLTAAPVLIRAVVQDMTL----------KMANGREYALRKGDRLALfPYL 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1217 VVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADM-------HTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPA 1289
Cdd:cd20633    345 AVQMDPEIHPEPHTFKYDRFL--NPDGGKKKDFYkngkklkYYNMPWGAGVSICPGRFFAVNEMKQFVFLMLTYFDLELV 422
                          250       260
                   ....*....|....*....|....*..
gi 1834010771 1290 SGKEfAIP---GHRPSSGAYLPKNDIK 1313
Cdd:cd20633    423 NPDE-EIPsidPSRWGFGTMQPTHDIQ 448
CYP7B1 cd20632
cytochrome P450 family 7, subfamily B, polypeptide 1; Cytochrome P450 7B1 (CYP7B1) is also ...
993-1312 2.38e-15

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: 80.81  E-value: 2.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  993 LLDDMWDFDNRFLAMSFGAPRWLplpgLSAAYAARDRILDAFaaYHQAFVSWDEGNDPgVKFRdlddvsepmKQRIRKFK 1072
Cdd:cd20632    146 LRKKFRKFDAMFPYLVANIPIEL----LGATKSIREKLIKYF--LPQKMAKWSNPSEV-IQAR---------QELLEQYD 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1073 ELGlsPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIApfaNAHRPSREETGLPFQepakISLDPDEL 1152
Cdd:cd20632    210 VLQ--DYDKAAHHFAFLWASVGNTIPATFWAMYYLLRHPEALAAVRDEID---HVLQSTGQELGPDFD----IHLTREQL 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1153 fRSCPLLKASFYETMRLDSAGLSFREVTSDLTVtespedaaaaNLGDPRTYRIKKGGNIIMAHGVVQRDPQLFSNPE--Q 1230
Cdd:cd20632    281 -DSLVYLESAINESLRLSSASMNIRVVQEDFTL----------KLESDGSVNLRKGDIVALYPQSLHMDPEIYEDPEvfK 349
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1231 FDplRFIvtdpDTGAQKADM--------HTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASG-KEFAIPGHRP 1301
Cdd:cd20632    350 FD--RFV----EDGKKKTTFykrgqklkYYLMPFGSGSSKCPGRFFAVNEIKQFLSLLLLYFDLELLEEqKPPGLDNSRA 423
                          330
                   ....*....|.
gi 1834010771 1302 SSGAYLPKNDI 1312
Cdd:cd20632    424 GLGILPPNSDV 434
CYP306A1-like cd20652
cytochrome P450 306A1 and similar cytochrome P450s; This subfamily is composed of insect and ...
1088-1307 6.79e-15

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: 79.38  E-value: 6.79e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1088 LFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRpsreetgLPFQEpakislDPDELfrscPLLKASFYETM 1167
Cdd:cd20652    242 LFGAGVDTTITTLRWFLLYMALFPKEQRRIQRELDEVVGRPD-------LVTLE------DLSSL----PYLQACISESQ 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1168 RLdsaglsfREVTSdLTVTESP-EDAaaaNLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDpdtGAQ 1246
Cdd:cd20652    305 RI-------RSVVP-LGIPHGCtEDA---VLAG---YRIPKGSMIIPLLWAVHMDPNLWEEPEEFRPERFLDTD---GKY 367
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834010771 1247 KADMHTIyPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEFaiPGHRPSSGAYL 1307
Cdd:cd20652    368 LKPEAFI-PFQTGKRMCLGDELARMILFLFTARILRKFRIALPDGQPV--DSEGGNVGITL 425
CYP51-like cd11042
cytochrome P450 family 51 and similar cytochrome P450s; This family is composed of cytochrome ...
982-1269 1.19e-14

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: 78.41  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  982 MGQAFLEafpNLLDDMW----DFDNRFLAMSFGAPrWLPLPglsaAYAARDRildAFAAYHQAFVSWDEgndpgvKFRDL 1057
Cdd:cd11042    123 LGKEVRE---LLDDEFAqlyhDLDGGFTPIAFFFP-PLPLP----SFRRRDR---ARAKLKEIFSEIIQ------KRRKS 185
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1058 DDVSEP------MKQRIRKFKELglsPRSSAPGHL-SLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRP 1130
Cdd:cd11042    186 PDKDEDdmlqtlMDAKYKDGRPL---TDDEIAGLLiALLFAGQHTSSATSAWTGLELLRNPEHLEALREEQKEVLGDGDD 262
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1131 SreetglpfqepakislDPDELFRSCPLLKASFYETMRLDSAGLS-FREVTSDLTVTESPedaaaanlgdprtYRIKKGg 1209
Cdd:cd11042    263 P----------------LTYDVLKEMPLLHACIKETLRLHPPIHSlMRKARKPFEVEGGG-------------YVIPKG- 312
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834010771 1210 NIIMAH-GVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADMHTIYPFGGGVSGCKGRALA 1269
Cdd:cd11042    313 HIVLASpAVSHRDPEIFKNPDEFDPERFL--KGRAEDSKGGKFAYLPFGAGRHRCIGENFA 371
CYP503A1-like cd11041
cytochrome P450 family 503, subfamily A, polypeptide 1 and similar cytochrome P450s; This ...
891-1294 1.80e-14

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: 78.10  E-value: 1.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  891 LSATDHHIIHHNIPNLLMREPFLTEAskaakdITERETPNLVTFCRSMVDqapWERRSEAEVIDGKEKPTaEVNLFALVR 970
Cdd:cd11041     46 EALEEHLAGFGTGGSVVLDSPLHVDV------VRKDLTPNLPKLLPDLQE---ELRAALDEELGSCTEWT-EVNLYDTVL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  971 NFVGHISTSV-----------------------SMGQAFLEAFPNLLddmwdfdNRFLAmsfgapRWLPLPGLSAAYAAR 1027
Cdd:cd11041    116 RIVARVSARVfvgpplcrneewldltinytidvFAAAAALRLFPPFL-------RPLVA------PFLPEPRRLRRLLRR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1028 -DRILDAFAAYHQAFVSWDEGNDPGVKFRDLDDVSEpmkqrirkfKELGLSPRSSApgHLSLFWALNA-NSPTVVFWHIL 1105
Cdd:cd11041    183 aRPLIIPEIERRRKLKKGPKEDKPNDLLQWLIEAAK---------GEGERTPYDLA--DRQLALSFAAiHTTSMTLTHVL 251
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1106 -RIYSDPALLEEIRKEIApfaNAHRPSREETglpfqepaKISLDpdelfrSCPLLKaSFY-ETMRLDSAGL--SFREVTS 1181
Cdd:cd11041    252 lDLAAHPEYIEPLREEIR---SVLAEHGGWT--------KAALN------KLKKLD-SFMkESQRLNPLSLvsLRRKVLK 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1182 DLTVTESpedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADMH---TIYP--- 1255
Cdd:cd11041    314 DVTLSDG--------------LTLPKGTRIAVPAHAIHRDPDIYPDPETFDGFRFY--RLREQPGQEKKHqfvSTSPdfl 377
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|
gi 1834010771 1256 -FGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEF 1294
Cdd:cd11041    378 gFGHGRHACPGRFFASNEIKLILAHLLLNYDFKLPEGGER 417
CYP132-like cd20620
cytochrome P450 family 132 and similar cytochrome P450s; This subfamily is composed of ...
988-1313 1.82e-14

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: 77.62  E-value: 1.82e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  988 EAFPNLLDDMwdfdNRFLAMSFGAPRWLPLPGLSAAYAAR---DRILDAFAAYHQAfvswdEGNDPGvkfrDL------- 1057
Cdd:cd20620    133 DALDVALEYA----ARRMLSPFLLPLWLPTPANRRFRRARrrlDEVIYRLIAERRA-----APADGG----DLlsmllaa 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1058 --DDVSEPM-KQRIRKfkELglsprssapghLSLFWA---LNANSPTVVFWHILRiysDPALLEEIRKEIAPFANAHRPS 1131
Cdd:cd20620    200 rdEETGEPMsDQQLRD--EV-----------MTLFLAgheTTANALSWTWYLLAQ---HPEVAARLRAEVDRVLGGRPPT 263
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1132 REEtglpfqepakisldpdelFRSCPLLKASFYETMRLDSAGLSF-REVTSDLTvtespedaaaanLGDprtYRIKKGGN 1210
Cdd:cd20620    264 AED------------------LPQLPYTEMVLQESLRLYPPAWIIgREAVEDDE------------IGG---YRIPAGST 310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1211 IIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDtgaQKADMH--TIYPFGGGVSGCKGR--ALAERTILLfsAAIISMWDI 1286
Cdd:cd20620    311 VLISPYVTHRDPRFWPDPEAFDPERF---TPE---REAARPryAYFPFGGGPRICIGNhfAMMEAVLLL--ATIAQRFRL 382
                          330       340       350
                   ....*....|....*....|....*....|
gi 1834010771 1287 EPAsgkefaiPGHRPSSGAYL---PKNDIK 1313
Cdd:cd20620    383 RLV-------PGQPVEPEPLItlrPKNGVR 405
CYP110-like cd11053
cytochrome P450 family 110 and similar cytochrome P450s; This group is composed of mostly ...
1102-1291 7.47e-14

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: 75.70  E-value: 7.47e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1102 WHILRIYSDPALLEEIRKEIApfanahrpsreeTGLPFQEPAKISLDPdelfrscpLLKASFYETMRL-DSAGLSFREVT 1180
Cdd:cd11053    245 WAFYWLHRHPEVLARLLAELD------------ALGGDPDPEDIAKLP--------YLDAVIKETLRLyPVAPLVPRRVK 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1181 SDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTgaqkadmHTIYPFGGGV 1260
Cdd:cd11053    305 EPVE------------LGG---YTLPAGTTVAPSIYLTHHRPDLYPDPERFRPERFLGRKPSP-------YEYLPFGGGV 362
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1834010771 1261 SGCKGRALA--ERTILLfsAAIISMWDIEPASG 1291
Cdd:cd11053    363 RRCIGAAFAllEMKVVL--ATLLRRFRLELTDP 393
PGIS_CYP8A1 cd20634
prostacyclin Synthase, also called cytochrome P450 family 8, subfamily A, polypeptide 1; ...
1069-1312 1.06e-13

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: 75.57  E-value: 1.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1069 RKFKELGLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIapfaNAHRPSREETGLPFQEPakisld 1148
Cdd:cd20634    210 LHLEEEGVDEEMQARAMLLQLWATQGNAGPAAFWLLLFLLKHPEAMAAVRGEI----QRIKHQRGQPVSQTLTI------ 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1149 PDELFRSCPLLKASFYETMRLDSAGLSFREVTSDLTVtespedaaaaNLGDPRTYRIKKGGNIIMAHGVV-QRDPQLFSN 1227
Cdd:cd20634    280 NQELLDNTPVFDSVLSETLRLTAAPFITREVLQDMKL----------RLADGQEYNLRRGDRLCLFPFLSpQMDPEIHQE 349
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1228 PEQFDPLRFIVTDpdtGAQKADMHT--------IYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASgKEFAIPGH 1299
Cdd:cd20634    350 PEVFKYDRFLNAD---GTEKKDFYKngkrlkyyNMPWGAGDNVCIGRHFAVNSIKQFVFLILTHFDVELKD-PEAEIPEF 425
                          250
                   ....*....|....*.
gi 1834010771 1300 RPSS---GAYLPKNDI 1312
Cdd:cd20634    426 DPSRygfGLLQPEGDI 441
CYP39A1 cd20635
cytochrome P450 family 39, subfamily A, polypeptide 1; Cytochrome P450 39A1 (CYP39A1) is also ...
1081-1287 1.26e-13

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: 75.04  E-value: 1.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1081 SAPGH-LSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIapfanahrpsREETGLPFQEPAKISLDpdeLFRSCPLL 1159
Cdd:cd20635    210 NAPNYsLLLLWASLANAIPITFWTLAFILSHPSVYKKVMEEI----------SSVLGKAGKDKIKISED---DLKKMPYI 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1160 KASFYETMRLDSAGLSFREVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVT 1239
Cdd:cd20635    277 KRCVLEAIRLRSPGAITRKVVKPIKIKN---------------YTIPAGDMLMLSPYWAHRNPKYFPDPELFKPERWKKA 341
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1834010771 1240 DPDtgaQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIE 1287
Cdd:cd20635    342 DLE---KNVFLEGFVAFGGGRYQCPGRWFALMEIQMFVAMFLYKYDFT 386
CYP1_2-like cd20617
cytochrome P450 families 1 and 2, and similar cytochrome P450s; This model includes cytochrome ...
1155-1292 4.62e-13

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: 73.40  E-value: 4.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1155 SCPLLKASFYETMRLDSAG-LSF-REVTSDLTVtespedaaaanlGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFD 1232
Cdd:cd20617    281 KLPYLNAVIKEVLRLRPILpLGLpRVTTEDTEI------------GG---YFIPKGTQIIINIYSLHRDEKYFEDPEEFN 345
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1233 PLRFIvtdpDTGAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGK 1292
Cdd:cd20617    346 PERFL----ENDGNKLSEQFI-PFGIGKRNCVGENLARDELFLFFANLLLNFKFKSSDGL 400
CYP24A1-like cd11054
cytochrome P450 family 24 subfamily A, polypeptide 1 and similar cytochrome P450s; This family ...
1151-1288 9.71e-13

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: 72.56  E-value: 9.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1151 ELFRSCPLLKASFYETMRLDS-AGLSFREVTSDLtvtespedaaaaNLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPE 1229
Cdd:cd11054    285 EDLKKMPYLKACIKESLRLYPvAPGNGRILPKDI------------VLSG---YHIPKGTLVVLSNYVMGRDEEYFPDPE 349
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1834010771 1230 QFDPLRFIvtDPDTGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEP 1288
Cdd:cd11054    350 EFIPERWL--RDDSENKNIHPFASLPFGFGPRMCIGRRFAELEMYLLLAKLLQNFKVEY 406
CYP11B cd20644
cytochrome P450 family 11, subfamily B subfamily; Cytochrome P450 11B (CYP11B) enzymes ...
1058-1293 6.99e-12

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: 69.87  E-value: 6.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1058 DDVSEPMKQRIRK-FKELGLSPRSSAPG---------HLSLFwALNANS--------PTVVF---WHILRIYSDPALLEE 1116
Cdd:cd20644    190 DCIFQYADNCIQKiYQELAFGRPQHYTGivaelllqaELSLE-AIKANIteltaggvDTTAFpllFTLFELARNPDVQQI 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1117 IRKEIAPFAnahrpsreetglpfqepAKISLDPDELFRSCPLLKASFYETMRLDSAGLSF-REVTSDLTVtespedaaaa 1195
Cdd:cd20644    269 LRQESLAAA-----------------AQISEHPQKALTELPLLKAALKETLRLYPVGITVqRVPSSDLVL---------- 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1196 nlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKAdmhtiYPFGGGVSGCKGRALAERTILL 1275
Cdd:cd20644    322 -----QNYHIPAGTLVQVFLYSLGRSAALFPRPERYDPQRWLDIRGSGRNFKH-----LAFGFGMRQCLGRRLAEAEMLL 391
                          250
                   ....*....|....*...
gi 1834010771 1276 FSAAIISMWDIEPASGKE 1293
Cdd:cd20644    392 LLMHVLKNFLVETLSQED 409
CYP11A1 cd20643
cytochrome P450 family 11, subfamily A, polypeptide 1, also called cholesterol side-chain ...
1098-1287 7.93e-12

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: 69.74  E-value: 7.93e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1098 TVVFWHILRIYSDPALLEEIRKEIApfaNAHRpsrEETGlpfqepakislDPDELFRSCPLLKASFYETMRLDSAGLSF- 1176
Cdd:cd20643    252 MTLQWTLYELARNPNVQEMLRAEVL---AARQ---EAQG-----------DMVKMLKSVPLLKAAIKETLRLHPVAVSLq 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1177 REVTSDLTVtespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDpdtgaqkadmhTIY-- 1254
Cdd:cd20643    315 RYITEDLVL---------------QNYHIPAGTLVQVGLYAMGRDPTVFPKPEKYDPERWLSKD-----------ITHfr 368
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1834010771 1255 --PFGGGVSGCKGRALAERTILLFSAAIISMWDIE 1287
Cdd:cd20643    369 nlGFGFGPRQCLGRRIAETEMQLFLIHMLENFKIE 403
CYP67-like cd11061
cytochrome P450 family 67 and similar cytochrome P450s; This subfamily includes Uromyces ...
1094-1293 2.83e-11

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: 67.63  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1094 ANSPTVVFWHILRiysDPALLEEIRKEIAPFanahrpsreetglpFQEPAKISLDPDelFRSCPLLKASFYETMRLDSAG 1173
Cdd:cd11061    233 ATALSAIFYYLAR---NPEAYEKLRAELDST--------------FPSDDEIRLGPK--LKSLPYLRACIDEALRLSPPV 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1174 LSF--REVTSD-LTVTES--PEDAaaaNLGDPrTYrikkggniimahgVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKA 1248
Cdd:cd11061    294 PSGlpRETPPGgLTIDGEyiPGGT---TVSVP-IY-------------SIHRDERYFPDPFEFIPERWLSRPEELVRARS 356
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1834010771 1249 dmhTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKE 1293
Cdd:cd11061    357 ---AFIPFSIGPRGCIGKNLAYMELRLVLARLLHRYDFRLAPGED 398
CYP_unk cd11083
unknown subfamily of cytochrome P450s; This subfamily is composed of uncharacterized ...
1102-1296 4.50e-11

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: 67.35  E-value: 4.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1102 WHILRIYSDPALLEEIRKEIapfanahrpsREETGlpfqePAKISLDPDELFRsCPLLKASFYETMRLDS-AGLSFREVT 1180
Cdd:cd11083    244 WMLYYLASRPDVQARVREEV----------DAVLG-----GARVPPLLEALDR-LPYLEAVARETLRLKPvAPLLFLEPN 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1181 SDLTVtespedaaaanlGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKADMHtiYPFGGGV 1260
Cdd:cd11083    308 EDTVV------------GD---IALPAGTPVFLLTRAAGLDAEHFPDPEEFDPERWLDGARAAEPHDPSSL--LPFGAGP 370
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1834010771 1261 SGCKGRALAERTILLFSAAIISMWDIE-----PASGKEFAI 1296
Cdd:cd11083    371 RLCPGRSLALMEMKLVFAMLCRNFDIElpepaPAVGEEFAF 411
CYP120A1_CYP26-like cd11044
cyanobacterial cytochrome P450 family 120, subfamily A, polypeptide 1 (CYP120A1), vertebrate ...
1132-1288 1.31e-10

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: 65.77  E-value: 1.31e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1132 REETG-LPFQEPakisLDPDELfRSCPLLKASFYETMRL-DSAGLSFREVTSDLtvtespedaaaaNLGDprtYRIKKGG 1209
Cdd:cd11044    261 RQEQDaLGLEEP----LTLESL-KKMPYLDQVIKEVLRLvPPVGGGFRKVLEDF------------ELGG---YQIPKGW 320
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1210 NIIMAHGVVQRDPQLFSNPEQFDPLRFivTDPDTGAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIIS--MWDIE 1287
Cdd:cd11044    321 LVYYSIRDTHRDPELYPDPERFDPERF--SPARSEDKKKPFSLI-PFGGGPRECLGKEFAQLEMKILASELLRnyDWELL 397

                   .
gi 1834010771 1288 P 1288
Cdd:cd11044    398 P 398
CYP64-like cd11065
cytochrome P450 family 64-like fungal cytochrome P450s; This group includes Aspergillus flavus ...
1203-1289 1.97e-10

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: 65.29  E-value: 1.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvTDPDTGAQKADMHTiYPFGGGVSGCKGRALAERTILLFSAAIIS 1282
Cdd:cd11065    316 YFIPKGTTVIPNAWAIHHDPEVYPDPEEFDPERYL-DDPKGTPDPPDPPH-FAFGFGRRICPGRHLAENSLFIAIARLLW 393

                   ....*..
gi 1834010771 1283 MWDIEPA 1289
Cdd:cd11065    394 AFDIKKP 400
CypX COG2124
Cytochrome P450 [Secondary metabolites biosynthesis, transport and catabolism, Defense ...
1157-1309 2.24e-10

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: 64.91  E-value: 2.24e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDS-AGLSFREVTSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLR 1235
Cdd:COG2124    268 ELLPAAVEETLRLYPpVPLLPRTATEDVE------------LGG---VTIPAGDRVLLSLAAANRDPRVFPDPDRFDPDR 332
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1834010771 1236 fivtdpdtgaqkaDMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMW-DIEPASGKEfaiPGHRPSSGAYLPK 1309
Cdd:COG2124    333 -------------PPNAHLPFGGGPHRCLGAALARLEARIALATLLRRFpDLRLAPPEE---LRWRPSLTLRGPK 391
CYP_fungal cd11059
unknown subfamily of fungal cytochrome P450s; This subfamily is composed of uncharacterized ...
951-1292 4.64e-10

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: 63.86  E-value: 4.64e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  951 EVIDGKEKPTAEVNLFALVRNFVGHISTSVSMGQAFL-------EAFPNLLDDMWDFDNRFLAMSFgaPRWLPLPG---- 1019
Cdd:cd11059     89 DRIAKEAGKSGSVDVYPLFTALAMDVVSHLLFGESFGtlllgdkDSRERELLRRLLASLAPWLRWL--PRYLPLATsrli 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1020 LSAAYAARDRI----LDAFAAYHQAFVSWDEGNDPGVKFRDLDDVSepmKQRIRKFKELglspRSSAPGHLSlfwalnAN 1095
Cdd:cd11059    167 IGIYFRAFDEIeewaLDLCARAESSLAESSDSESLTVLLLEKLKGL---KKQGLDDLEI----ASEALDHIV------AG 233
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1096 SPTV------VFWHILRiysDPALLEEIRKEIApfanahrpsreetGLPfqEPAKISLDPDELfRSCPLLKASFYETMRL 1169
Cdd:cd11059    234 HDTTavtltyLIWELSR---PPNLQEKLREELA-------------GLP--GPFRGPPDLEDL-DKLPYLNAVIRETLRL 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1170 dsaglsfrevtsdltvtespedAAAANLGDPRtyRIKKGGNIIMAH----GVV--------QRDPQLFSNPEQFDPLRFI 1237
Cdd:cd11059    295 ----------------------YPPIPGSLPR--VVPEGGATIGGYyipgGTIvstqayslHRDPEVFPDPEEFDPERWL 350
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834010771 1238 vtdPDTGAQKADMHT-IYPFGGGVSGCKGRALAERTILLFSAAI----------------ISMWDIEPASGK 1292
Cdd:cd11059    351 ---DPSGETAREMKRaFWPFGSGSRMCIGMNLALMEMKLALAAIyrnyrtstttdddmeqEDAFLAAPKGRR 419
CYP90-like cd11043
plant cytochrome P450s similar to cytochrome P450 family 90, subfamily A, polypeptide 1, ...
1164-1276 1.72e-09

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: 62.20  E-value: 1.72e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1164 YETMRLDS-AGLSFREVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFivtdpd 1242
Cdd:cd11043    280 NETLRLAPiVPGVFRKALQDVEYKG---------------YTIPKGWKVLWSARATHLDPEYFPDPLKFNPWRW------ 338
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1834010771 1243 tgaQKADMHTIY---PFGGGVSGCKGRALAERTILLF 1276
Cdd:cd11043    339 ---EGKGKGVPYtflPFGGGPRLCPGAELAKLEILVF 372
CYP170A1-like cd11049
cytochrome P450 family 170, subfamily A, polypeptide 1-like actinobacterial cytochrome P450s; ...
1165-1307 2.99e-09

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: 61.51  E-value: 2.99e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDSAGLSF-REVTSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDT 1243
Cdd:cd11049    287 EALRLYPPVWLLtRRTTADVE------------LGG---HRLPAGTEVAFSPYALHRDPEVYPDPERFDPDRW---LPGR 348
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834010771 1244 GAQKADMHTIyPFGGGVSGCKGR--ALAERTILLfsAAIISMWDIEPASGkefaiPGHRPSSGAYL 1307
Cdd:cd11049    349 AAAVPRGAFI-PFGAGARKCIGDtfALTELTLAL--ATIASRWRLRPVPG-----RPVRPRPLATL 406
CYP6-like cd11056
cytochrome P450 family 6 and similar cytochrome P450s; This family is composed of cytochrome ...
1159-1313 4.23e-09

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: 61.02  E-value: 4.23e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1159 LKASFYETMRLDS-AGLSFREVTSDLTVTESPedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFI 1237
Cdd:cd11056    292 LDQVVNETLRKYPpLPFLDRVCTKDYTLPGTD-------------VVIEKGTPVIIPVYALHHDPKYYPEPEKFDPERFS 358
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1238 vtdpDTGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPAsgKEFAIPGH-RPSSGAYLPKNDIK 1313
Cdd:cd11056    359 ----PENKKKRHPYTYLPFGDGPRNCIGMRFGLLQVKLGLVHLLSNFRVEPS--SKTKIPLKlSPKSFVLSPKGGIW 429
CYP82 cd20654
cytochrome P450 family 82; Cytochrome P450 family 82 (CYP82 or Cyp82) genes specifically ...
1159-1291 9.93e-09

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: 59.94  E-value: 9.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1159 LKASFYETMRLDSAG--LSFREVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRF 1236
Cdd:cd20654    303 LQAIVKETLRLYPPGplLGPREATEDCTVGG---------------YHVPKGTRLLVNVWKIQRDPNVWSDPLEFKPERF 367
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1834010771 1237 IVTDPDTGAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASG 1291
Cdd:cd20654    368 LTTHKDIDVRGQNFELI-PFGSGRRSCPGVSFGLQVMHLTLARLLHGFDIKTPSN 421
CYP17A1-like cd11027
cytochrome P450 family 17, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
1155-1291 1.16e-08

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: 59.53  E-value: 1.16e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1155 SCPLLKASFYETMRLDS-AGLSF-REVTSDLTVtespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFD 1232
Cdd:cd11027    287 RLPYLEATIAEVLRLSSvVPLALpHKTTCDTTL---------------RGYTIPKGTTVLVNLWALHHDPKEWDDPDEFR 351
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1834010771 1233 PLRFIvtDPDtGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASG 1291
Cdd:cd11027    352 PERFL--DEN-GKLVPKPESFLPFSAGRRVCLGESLAKAELFLFLARLLQKFRFSPPEG 407
CYP136-like cd11045
putative cytochrome P450 family 136 and similar cytochrome P450s; This group is composed of ...
1157-1276 1.25e-08

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: 59.25  E-value: 1.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDS-AGLSFREVTSDLTVtespedaaaanLGdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLR 1235
Cdd:cd11045    269 EVTDWVFKEALRLVPpVPTLPRRAVKDTEV-----------LG----YRIPAGTLVAVSPGVTHYMPEYWPNPERFDPER 333
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1834010771 1236 FivtDPDTGAQKADMHTIYPFGGGVSGCKGRALAERTILLF 1276
Cdd:cd11045    334 F---SPERAEDKVHRYAWAPFGGGAHKCIGLHFAGMEVKAI 371
CYP74 cd11071
cytochrome P450 family 74; The cytochrome P450 74 (CYP74) family controls several enzymatic ...
1088-1281 1.54e-08

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: 59.20  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1088 LFWALNANS--------PTVVFWhilrIYSDPA-----LLEEIRKEIapfanahrpsREETGLPFQepakiSLDpdELfr 1154
Cdd:cd11071    229 LLFMLGFNAfggfsallPSLLAR----LGLAGEelharLAEEIRSAL----------GSEGGLTLA-----ALE--KM-- 285
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1155 scPLLKASFYETMRLD-SAGLSFREVTSDLTVtESpEDAAaanlgdprtYRIKKG----GNIIMAHgvvqRDPQLFSNPE 1229
Cdd:cd11071    286 --PLLKSVVYETLRLHpPVPLQYGRARKDFVI-ES-HDAS---------YKIKKGellvGYQPLAT----RDPKVFDNPD 348
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834010771 1230 QFDPLRFIVTD------------PDTGAQKADMHTiypfgggvsgCKGRALAERTILLFSAAII 1281
Cdd:cd11071    349 EFVPDRFMGEEgkllkhliwsngPETEEPTPDNKQ----------CPGKDLVVLLARLFVAELF 402
PLN02196 PLN02196
abscisic acid 8'-hydroxylase
1075-1297 2.68e-08

abscisic acid 8'-hydroxylase


Pssm-ID: 177847 [Multi-domain]  Cd Length: 463  Bit Score: 58.41  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1075 GLSPRSSAPGHLSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFAnahRPSREETGLPFQEPAKIsldpdelfr 1154
Cdd:PLN02196   259 GLTDEQIADNIIGVIFAARDTTASVLTWILKYLAENPSVLEAVTEEQMAIR---KDKEEGESLTWEDTKKM--------- 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1155 scPLLKASFYETMRLDSAgLSFrevtsdlTVTESPEDAaaanlgDPRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPL 1234
Cdd:PLN02196   327 --PLTSRVIQETLRVASI-LSF-------TFREAVEDV------EYEGYLIPKGWKVLPLFRNIHHSADIFSDPGKFDPS 390
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834010771 1235 RFIVtdpdtgAQKADmhTIYPFGGGVSGCKGRALA--ERTILLFSAAIISMWDI-EPASGKE---FAIP 1297
Cdd:PLN02196   391 RFEV------APKPN--TFMPFGNGTHSCPGNELAklEISVLIHHLTTKYRWSIvGTSNGIQygpFALP 451
CYP17A1 cd20673
cytochrome P450 family 17, subfamily A, polypeptide 1; Cytochrome P450 17A1 (CYP17A1 or ...
1098-1292 6.70e-08

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: 57.33  E-value: 6.70e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1098 TVVFWHILRIYSDPALLEEIRKEIapfanahrpsreETGLPFQEPAKISlDPDELfrscPLLKASFYETMRldsaglsFR 1177
Cdd:cd20673    250 TVLKWIIAFLLHNPEVQKKIQEEI------------DQNIGFSRTPTLS-DRNHL----PLLEATIREVLR-------IR 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1178 EVTSDLTvtesPEDAAA-ANLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPdTGAQKADMHTIY-P 1255
Cdd:cd20673    306 PVAPLLI----PHVALQdSSIGE---FTIPKGTRVVINLWALHHDEKEWDQPDQFMPERFL--DP-TGSQLISPSLSYlP 375
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1834010771 1256 FGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGK 1292
Cdd:cd20673    376 FGAGPRVCLGEALARQELFLFMAWLLQRFDLEVPDGG 412
PLN02687 PLN02687
flavonoid 3'-monooxygenase
1086-1291 7.87e-08

flavonoid 3'-monooxygenase


Pssm-ID: 215371 [Multi-domain]  Cd Length: 517  Bit Score: 57.13  E-value: 7.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1086 LSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRPSREetglpfqepakisLDPDELfrscPLLKASFYE 1165
Cdd:PLN02687   303 LNLFTAGTDTTSSTVEWAIAELIRHPDILKKAQEELDAVVGRDRLVSE-------------SDLPQL----TYLQAVIKE 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1166 TMRLD-SAGLSFREVTSdltvtESPEDAAaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIV--TDPD 1242
Cdd:PLN02687   366 TFRLHpSTPLSLPRMAA-----EECEING---------YHIPKGATLLVNVWAIARDPEQWPDPLEFRPDRFLPggEHAG 431
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1834010771 1243 TGAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASG 1291
Cdd:PLN02687   432 VDVKGSDFELI-PFGAGRRICAGLSWGLRMVTLLTATLVHAFDWELADG 479
RRM_1 pfam00076
RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic ...
202-258 1.62e-07

RNA recognition motif. (a.k.a. RRM, RBD, or RNP domain); The RRM motif is probably diagnostic of an RNA binding protein. RRMs are found in a variety of RNA binding proteins, including various hnRNP proteins, proteins implicated in regulation of alternative splicing, and protein components of snRNPs. The motif also appears in a few single stranded DNA binding proteins. The RRM structure consists of four strands and two helices arranged in an alpha/beta sandwich, with a third helix present during RNA binding in some cases The C-terminal beta strand (4th strand) and final helix are hard to align and have been omitted in the SEED alignment The LA proteins have an N terminal rrm which is included in the seed. There is a second region towards the C terminus that has some features characteriztic of a rrm but does not appear to have the important structural core of a rrm. The LA proteins are one of the main autoantigens in Systemic lupus erythematosus (SLE), an autoimmune disease.


Pssm-ID: 425453 [Multi-domain]  Cd Length: 70  Bit Score: 49.92  E-value: 1.62e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771  202 DLNTETLYTLFRPYGKIRDIEKQPSDSKVTPRYAFVEFSRPKYAGMAKNCMHGFTVP 258
Cdd:pfam00076    9 DTTEEDLKDLFSKFGPIKSIRLVRDETGRSKGFAFVEFEDEEDAEKAIEALNGKELG 65
RRM_SF cd00590
RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP ...
202-273 3.21e-07

RNA recognition motif (RRM) superfamily; RRM, also known as RBD (RNA binding domain) or RNP (ribonucleoprotein domain), is a highly abundant domain in eukaryotes found in proteins involved in post-transcriptional gene expression processes including mRNA and rRNA processing, RNA export, and RNA stability. This domain is 90 amino acids in length and consists of a four-stranded beta-sheet packed against two alpha-helices. RRM usually interacts with ssRNA, but is also known to interact with ssDNA as well as proteins. RRM binds a variable number of nucleotides, ranging from two to eight. The active site includes three aromatic side-chains located within the conserved RNP1 and RNP2 motifs of the domain. The RRM domain is found in a variety heterogeneous nuclear ribonucleoproteins (hnRNPs), proteins implicated in regulation of alternative splicing, and protein components of small nuclear ribonucleoproteins (snRNPs).


Pssm-ID: 409669 [Multi-domain]  Cd Length: 72  Bit Score: 49.20  E-value: 3.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834010771  202 DLNTETLYTLFRPYGKIRDIEKQPSDSKVTPRYAFVEFSRPKYAGMAKNCMHGftvpeQEGGGKsgtRLKIK 273
Cdd:cd00590      9 DTTEEDLRELFSKFGEVVSVRIVRDRDGKSKGFAFVEFESPEDAEKALEALNG-----TELGGR---PLKVS 72
CYP77_89 cd11075
cytochrome P450 families 77 and 89, and similar cytochrome P450s; This group includes ...
1086-1269 3.43e-07

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: 54.94  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1086 LSLFW-ALNANSPTVVF---WHILRIYSDPALLEEIRKEIAPFANAHRPSREEtglpfqepakislDPDELfrscPLLKA 1161
Cdd:cd11075    233 VSLCSeFLNAGTDTTATaleWAMAELVKNPEIQEKLYEEIKEVVGDEAVVTEE-------------DLPKM----PYLKA 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1162 SFYETMRLDSAG--LSFREVTSDLTvtespedaaaanLGDprtYRIKKGGNI-IMAHGVvQRDPQLFSNPEQFDPLRFI- 1237
Cdd:cd11075    296 VVLETLRRHPPGhfLLPHAVTEDTV------------LGG---YDIPAGAEVnFNVAAI-GRDPKVWEDPEEFKPERFLa 359
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1834010771 1238 ---VTDPDTGaqkADMHTIYPFGGGVSGCKGRALA 1269
Cdd:cd11075    360 ggeAADIDTG---SKEIKMMPFGAGRRICPGLGLA 391
CYP76-like cd11073
cytochrome P450 family 76 and similar cytochrome P450s; Characterized members of the plant ...
1157-1281 4.02e-07

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: 54.85  E-value: 4.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDSAG--LSFREVTSDLTVtespedaaaanLGdprtYRIKKGGNIIM-AHGVvQRDPQLFSNPEQFDP 1233
Cdd:cd11073    291 PYLQAVVKETLRLHPPAplLLPRKAEEDVEV-----------MG----YTIPKGTQVLVnVWAI-GRDPSVWEDPLEFKP 354
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1834010771 1234 LRFIVTDPDTGAQkaDMHTIyPFGGGVSGCKGRALAERTILLFSAAII 1281
Cdd:cd11073    355 ERFLGSEIDFKGR--DFELI-PFGSGRRICPGLPLAERMVHLVLASLL 399
CYP15A1-like cd20651
cytochrome P450 family 15, subfamily A, polypeptide 1, and similar cytochrome P450s; This ...
1203-1292 5.53e-07

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: 54.15  E-value: 5.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDtGAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIIS 1282
Cdd:cd20651    318 YRIPKDTTILASLYSVHMDPEYWGDPEEFRPERFL--DED-GKLLKDEWFL-PFGAGKRRCLGESLARNELFLFFTGLLQ 393
                           90
                   ....*....|
gi 1834010771 1283 MWDIEPASGK 1292
Cdd:cd20651    394 NFTFSPPNGS 403
CYP_LDS-like_C cd20612
C-terminal cytochrome P450 domain of linoleate diol synthase and similar cytochrome P450s; ...
1158-1308 6.32e-07

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


Pssm-ID: 410705 [Multi-domain]  Cd Length: 370  Bit Score: 53.88  E-value: 6.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1158 LLKASFYETMRLD-SAGLSFREVTSDLTVTEspedaaaanlGDPRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRf 1236
Cdd:cd20612    239 TLRGYVLEALRLNpIAPGLYRRATTDTTVAD----------GGGRTVSIKAGDRVFVSLASAMRDPRAFPDPERFRLDR- 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1237 ivtdPDTgaqkADMHtiypFGGGVSGCKGRALAErtillfsAAIISMW-------DIEPASGKEFAI-PGHRPSSGAYLP 1308
Cdd:cd20612    308 ----PLE----SYIH----FGHGPHQCLGEEIAR-------AALTEMLrvvlrlpNLRRAPGPQGELkKIPRGGFKAYLR 368
CYP1 cd11028
cytochrome P450 family 1; The cytochrome P450 family 1 (CYP1 or Cyp1) is composed of three ...
1098-1281 7.86e-07

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: 53.84  E-value: 7.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1098 TVVFWHILRIYSDPALLEEIRKEIAPFANAHRPSREEtglpfqepakislDPDELfrscPLLKASFYETMRLdSAGLSF- 1176
Cdd:cd11028    249 TTLQWSLLYMIRYPEIQEKVQAELDRVIGRERLPRLS-------------DRPNL----PYTEAFILETMRH-SSFVPFt 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1177 --REVTSDLTVtespedaaaanLGdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADMHTIY 1254
Cdd:cd11028    311 ipHATTRDTTL-----------NG----YFIPKGTVVFVNLWSVNHDEKLWPDPSVFRPERFL--DDNGLLDKTKVDKFL 373
                          170       180
                   ....*....|....*....|....*..
gi 1834010771 1255 PFGGGVSGCKGRALAERTILLFSAAII 1281
Cdd:cd11028    374 PFGAGRRRCLGEELARMELFLFFATLL 400
CYP4V cd20680
cytochrome P450 family 4, subfamily V; Cytochrome P450 family 4, subfamily V, polypeptide 2 ...
1102-1293 1.28e-06

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: 53.23  E-value: 1.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1102 WHILRIYSDPALLEEIRKEIAP-FANAHRPsreetglpfqepakISLDPDELFRscpLLKASFYETMRL-DSAGLSFREV 1179
Cdd:cd20680    265 WSLYLLGSHPEVQRKVHKELDEvFGKSDRP--------------VTMEDLKKLR---YLECVIKESLRLfPSVPLFARSL 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1180 TSDLTVtespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdPDTgAQKADMHTIYPFGGG 1259
Cdd:cd20680    328 CEDCEI---------------RGFKVPKGVNAVIIPYALHRDPRYFPEPEEFRPERFF---PEN-SSGRHPYAYIPFSAG 388
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1834010771 1260 VSGCKGRALA---ERTILlfsAAIISMWDIEPASGKE 1293
Cdd:cd20680    389 PRNCIGQRFAlmeEKVVL---SCILRHFWVEANQKRE 422
PTZ00404 PTZ00404
cytochrome P450; Provisional
1086-1292 1.35e-06

cytochrome P450; Provisional


Pssm-ID: 173595 [Multi-domain]  Cd Length: 482  Bit Score: 53.19  E-value: 1.35e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1086 LSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRpsreetglpfqepaKISLDPDElfrSCPLLKASFYE 1165
Cdd:PTZ00404   289 LDFFLAGVDTSATSLEWMVLMLCNYPEIQEKAYNEIKSTVNGRN--------------KVLLSDRQ---STPYTVAIIKE 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1166 TMRLD---SAGLSfREVTSDLTVTESpedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDpd 1242
Cdd:PTZ00404   352 TLRYKpvsPFGLP-RSTSNDIIIGGG--------------HFIPKDAQILINYYSLGRNEKYFENPEQFDPSRFLNPD-- 414
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1243 tgaqkaDMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGK 1292
Cdd:PTZ00404   415 ------SNDAFMPFSIGPRNCVGQQFAQDELYLAFSNIILNFKLKSIDGK 458
CYPBJ-4-like cd20614
cytochrome P450 BJ-4 homolog and similar cytochrome P450s; This group is composed of mostly ...
1149-1308 1.65e-06

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: 52.83  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1149 PDELFRSCPLLKASFYETMRLDSA-GLSFREVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSN 1227
Cdd:cd20614    258 TPAELRRFPLAEALFRETLRLHPPvPFVFRRVLEEIELGG---------------RRIPAGTHLGIPLLLFSRDPELYPD 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1228 PEQFDPLRFI-VTDPDTGAQKADmhtiypFGGGVSGCKGRALAERTILLFSAAIISMWdiePASGKEFAIPGHRPSSgAY 1306
Cdd:cd20614    323 PDRFRPERWLgRDRAPNPVELLQ------FGGGPHFCLGYHVACVELVQFIVALAREL---GAAGIRPLLVGVLPGR-RY 392

                   ..
gi 1834010771 1307 LP 1308
Cdd:cd20614    393 FP 394
CYP5011A1-like cd20621
cytochrome P450 monooxygenase CYP5011A1 and similar cytochrome P450s; This subfamily is ...
1157-1269 1.72e-06

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: 52.64  E-value: 1.72e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLD--SAGLSFREVTSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPL 1234
Cdd:cd20621    289 NYLNAFIKEVLRLYnpAPFLFPRVATQDHQ------------IGD---LKIKKGWIVNVGYIYNHFNPKYFENPDEFNPE 353
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1834010771 1235 RFIvtdpdTGAQKADMHTIY-PFGGGVSGCKGRALA 1269
Cdd:cd20621    354 RWL-----NQNNIEDNPFVFiPFSAGPRNCIGQHLA 384
CYP58-like cd11062
cytochrome P450 family 58-like fungal cytochrome P450s; This group includes Fusarium ...
1094-1287 1.84e-06

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: 52.64  E-value: 1.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1094 ANSPTVVFWHILriySDPALLEEIRKEIapfanahrpsreETGLPfqePAKISLDPDELfRSCPLLKASFYETMRLdSAG 1173
Cdd:cd11062    241 ARTLSVATFHLL---SNPEILERLREEL------------KTAMP---DPDSPPSLAEL-EKLPYLTAVIKEGLRL-SYG 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1174 lsfreVTSDLTVTeSPEDAAAANlgdprTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvTDPDTGAQKadmHTI 1253
Cdd:cd11062    301 -----VPTRLPRV-VPDEGLYYK-----GWVIPPGTPVSMSSYFVHHDEEIFPDPHEFRPERWL-GAAEKGKLD---RYL 365
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1834010771 1254 YPFGGGVSGCKGRALAERTILLFSAAIISMWDIE 1287
Cdd:cd11062    366 VPFSKGSRSCLGINLAYAELYLALAALFRRFDLE 399
CYP3A-like cd11055
cytochrome P450 family 3, subfamily A and similar cytochrome P450s; This family includes ...
1165-1269 2.46e-06

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: 52.20  E-value: 2.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDSAGLSF-REVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFivTDPDT 1243
Cdd:cd11055    294 ETLRLYPPAFFIsRECKEDCTING---------------VFIPKGVDVVIPVYAIHHDPEFWPDPEKFDPERF--SPENK 356
                           90       100
                   ....*....|....*....|....*.
gi 1834010771 1244 gaQKADMHTIYPFGGGVSGCKGRALA 1269
Cdd:cd11055    357 --AKRHPYAYLPFGAGPRNCIGMRFA 380
CYP75 cd20657
cytochrome P450 family 75; The cytochrome P450 family 75 (CYP75) play important roles in the ...
1086-1291 2.55e-06

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: 52.04  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1086 LSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRPsREETGLPfqepakisldpdelfrSCPLLKASFYE 1165
Cdd:cd20657    234 LNLFTAGTDTSSSTVEWALAELIRHPDILKKAQEEMDQVIGRDRR-LLESDIP----------------NLPYLQAICKE 296
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1166 TMRLD-SAGLSFREVTSdltvtESPEDAAaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIV-TDPDT 1243
Cdd:cd20657    297 TFRLHpSTPLNLPRIAS-----EACEVDG---------YYIPKGTRLLVNIWAIGRDPDVWENPLEFKPERFLPgRNAKV 362
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1834010771 1244 GAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASG 1291
Cdd:cd20657    363 DVRGNDFELI-PFGAGRRICAGTRMGIRMVEYILATLVHSFDWKLPAG 409
CYP120A1 cd11068
cytochrome P450 family 102, subfamily A, polypeptide 1, also called bifunctional cytochrome ...
1157-1288 2.64e-06

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: 52.19  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRL-DSAGLSFREVTSDLTvtespedaaaanLGDPrtYRIKKGGNIIMAHGVVQRDPQLF-SNPEQFDPL 1234
Cdd:cd11068    289 RYIRRVLDETLRLwPTAPAFARKPKEDTV------------LGGK--YPLKKGDPVLVLLPALHRDPSVWgEDAEEFRPE 354
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1834010771 1235 RFivtDPDtGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEP 1288
Cdd:cd11068    355 RF---LPE-EFRKLPPNAWKPFGNGQRACIGRQFALQEATLVLAMLLQRFDFED 404
CYP56-like cd11070
cytochrome P450 family 56-like fungal cytochrome P450s; This group includes Saccharomyces ...
1140-1277 2.76e-06

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: 51.95  E-value: 2.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1140 QEPAKISLDPDELFRSCPLLKASFYETMRL-DSAGLSFREVTSDLTVTEspedaaaanlGDPRTYRIKKGGNI-IMAHGv 1217
Cdd:cd11070    268 LGDEPDDWDYEEDFPKLPYLLAVIYETLRLyPPVQLLNRKTTEPVVVIT----------GLGQEIVIPKGTYVgYNAYA- 336
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1218 VQRDPQL-FSNPEQFDPLRFIVTDPDTGA----QKADMHTIyPFGGGVSGCKGR--ALAERTILLFS 1277
Cdd:cd11070    337 THRDPTIwGPDADEFDPERWGSTSGEIGAatrfTPARGAFI-PFSAGPRACLGRkfALVEFVAALAE 402
PLN02302 PLN02302
ent-kaurenoic acid oxidase
1165-1315 3.13e-06

ent-kaurenoic acid oxidase


Pssm-ID: 215171 [Multi-domain]  Cd Length: 490  Bit Score: 52.02  E-value: 3.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDSAGL-SFREVTSDLTVTespedaaaanlgdprTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPdt 1243
Cdd:PLN02302   359 ETLRLINISLtVFREAKTDVEVN---------------GYTIPKGWKVLAWFRQVHMDPEVYPNPKEFDPSRWDNYTP-- 421
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834010771 1244 gaqKAdmHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASgkefaiPGHRPSsgaYLPKNDIKDN 1315
Cdd:PLN02302   422 ---KA--GTFLPFGLGSRLCPGNDLAKLEISIFLHHFLLGYRLERLN------PGCKVM---YLPHPRPKDN 479
CYP97 cd11046
cytochrome P450 family/clan 97; CYPs have been classified into families and subfamilies based ...
1203-1298 3.22e-06

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: 51.98  E-value: 3.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKADMHTIYPFGGGVSGCKGR--ALAERTILLfsAAI 1280
Cdd:cd11046    334 VKVPAGTDIFISVYNLHRSPELWEDPEEFDPERFLDPFINPPNEVIDDFAFLPFGGGPRKCLGDqfALLEATVAL--AML 411
                           90       100
                   ....*....|....*....|
gi 1834010771 1281 ISMWDIEPASGKE--FAIPG 1298
Cdd:cd11046    412 LRRFDFELDVGPRhvGMTTG 431
CYP27B1 cd20648
cytochrome P450 family 27, subfamily B, polypeptide 1, also called calcidiol 1-monooxygenase; ...
1157-1291 3.86e-06

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: 51.68  E-value: 3.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDSAGLSFREVTSDLTVtespedaaaaNLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRF 1236
Cdd:cd20648    294 PLLKAVVKEVLRLYPVIPGNARVIPDRDI----------QVGE---YIIPKKTLITLCHYATSRDENQFPDPNSFRPERW 360
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834010771 1237 IvtdpdtgaQKADMHTIY---PFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASG 1291
Cdd:cd20648    361 L--------GKGDTHHPYaslPFGFGKRSCIGRRIAELEVYLALARILTHFEVRPEPG 410
CYP5A1 cd20649
cytochrome P450 family 5, subfamily A, polypeptide 1, also called thromboxane-A synthase; ...
1157-1312 4.25e-06

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: 51.38  E-value: 4.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDSAGLSF-REVTSDLTVtespedaaaanLGDprtyRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLR 1235
Cdd:cd20649    321 PYLDMVIAETLRMYPPAFRFaREAAEDCVV-----------LGQ----RIPAGAVLEIPVGFLHHDPEHWPEPEKFIPER 385
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834010771 1236 FivtdpdTGAQKADMH--TIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEfaIPGHRPSSGAYLPKNDI 1312
Cdd:cd20649    386 F------TAEAKQRRHpfVYLPFGAGPRSCIGMRLALLEIKVTLLHILRRFRFQACPETE--IPLQLKSKSTLGPKNGV 456
Cyp2F cd20669
cytochrome P450 family 2, subfamily F; Cytochrome P450 family 2, subfamily F (CYP2F) members ...
1201-1288 4.32e-06

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: 51.30  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1201 RTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADmhTIYPFGGGVSGCKGRALAERTILLFSAAI 1280
Cdd:cd20669    317 RGFLIPKGTDVIPLLNSVHYDPTQFKDPQEFNPEHFL--DDNGSFKKND--AFMPFSAGKRICLGESLARMELFLYLTAI 392

                   ....*...
gi 1834010771 1281 ISMWDIEP 1288
Cdd:cd20669    393 LQNFSLQP 400
CYP27A1 cd20646
cytochrome P450 family 27, subfamily A, polypeptide 1, also called vitamin D(3) 25-hydroxylase; ...
1151-1293 4.65e-06

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: 51.20  E-value: 4.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1151 ELFRSCPLLKASFYETMRLdsaglsFREVTSDLTVTESPEdaaaANLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQ 1230
Cdd:cd20646    287 EDIAKMPLLKAVIKETLRL------YPVVPGNARVIVEKE----VVVGD---YLFPKNTLFHLCHYAVSHDETNFPEPER 353
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1231 FDPLRFIvtdpdtgAQKADMHTIY---PFGGGVSGCKGRALAERTILLFSAAIISMWDIEPA-SGKE 1293
Cdd:cd20646    354 FKPERWL-------RDGGLKHHPFgsiPFGYGVRACVGRRIAELEMYLALSRLIKRFEVRPDpSGGE 413
CYP86A cd11064
cytochrome P450 family 86, subfamily A; This subfamily includes several Arabidopsis thaliana ...
1088-1295 4.82e-06

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: 51.05  E-value: 4.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1088 LFWALNANsPTVvfwhilriysdpalLEEIRKEIapfaNAHRPSREETGLpfqepakISLDPDELfRSCPLLKASFYETM 1167
Cdd:cd11064    253 FFWLLSKN-PRV--------------EEKIREEL----KSKLPKLTTDES-------RVPTYEEL-KKLVYLHAALSESL 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1168 RL-DSAGLSFREVTSDLTVtespedaaaanlgdPRTYRIKKGGNIIMAHGVVQRDPQLF-SNPEQFDPLRFIvtDPDTGA 1245
Cdd:cd11064    306 RLyPPVPFDSKEAVNDDVL--------------PDGTFVKKGTRIVYSIYAMGRMESIWgEDALEFKPERWL--DEDGGL 369
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1246 QKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEFA 1295
Cdd:cd11064    370 RPESPYKFPAFNAGPRICLGKDLAYLQMKIVAAAILRRFDFKVVPGHKVE 419
PLN02655 PLN02655
ent-kaurene oxidase
1102-1269 5.39e-06

ent-kaurene oxidase


Pssm-ID: 215354 [Multi-domain]  Cd Length: 466  Bit Score: 51.28  E-value: 5.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1102 WHILRIYSDPALLEEIRKEIAPFANAHRPSREEtgLPfqepakisldpdelfrSCPLLKASFYETMRLDSAG--LSFREV 1179
Cdd:PLN02655   284 WAMYELAKNPDKQERLYREIREVCGDERVTEED--LP----------------NLPYLNAVFHETLRKYSPVplLPPRFV 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1180 TSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdpDTGAQKADMHTIYPFGGG 1259
Cdd:PLN02655   346 HEDTT------------LGG---YDIPAGTQIAINIYGCNMDKKRWENPEEWDPERFL----GEKYESADMYKTMAFGAG 406
                          170
                   ....*....|
gi 1834010771 1260 VSGCKGRALA 1269
Cdd:PLN02655   407 KRVCAGSLQA 416
CYP4 cd20628
cytochrome P450 family 4; Cytochrome P450 family 4 (CYP4) proteins catalyze the ...
1165-1290 6.14e-06

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: 50.98  E-value: 6.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRL-DSAGLSFREVTSDLTVTEspedaaaanlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDT 1243
Cdd:cd20628    298 ETLRLyPSVPFIGRRLTEDIKLDG---------------YTIPKGTTVVISIYALHRNPEYFPDPEKFDPDRF---LPEN 359
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1834010771 1244 GAQKadmHTiY---PFGGGVSGCKGR--ALAERTILLfsAAIISMWDIEPAS 1290
Cdd:cd20628    360 SAKR---HP-YayiPFSAGPRNCIGQkfAMLEMKTLL--AKILRNFRVLPVP 405
CYP26C1 cd20636
cytochrome P450 family 26, subfamily C, polypeptide 1; Cytochrome P450 26C1 (CYP26C1) is a ...
1203-1290 1.13e-05

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: 50.22  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKadMHTIyPFGGGVSGCKGRALAERTILLFSAAIIS 1282
Cdd:cd20636    325 YQIPKGWSVMYSIRDTHETAAVYQNPEGFDPDRFGVEREESKSGR--FNYI-PFGGGVRSCIGKELAQVILKTLAVELVT 401

                   ....*...
gi 1834010771 1283 MWDIEPAS 1290
Cdd:cd20636    402 TARWELAT 409
CYP2U1 cd20666
cytochrome P450 family 2, subfamily U, polypeptide 1; CYP2U1 is a thymus- and brain-specific ...
956-1276 1.40e-05

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: 49.77  E-value: 1.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771  956 KEKPTAEVNLFALVRNFVGHISTSVSMGQAFL---EAFPNLLDDMwdfdNRFLAMSFGAP-------RWL---PLPGLSA 1022
Cdd:cd20666     98 LKHGGDPFNPFPIVNNAVSNVICSMSFGRRFDyqdVEFKTMLGLM----SRGLEISVNSAailvnicPWLyylPFGPFRE 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1023 AYAARDRI---LDAFAAYHQAfvSWDEGNDpgvkfRDLDDVSEPMKQRIRKfkelGLSPRSSAPGHL-----SLFWALNA 1094
Cdd:cd20666    174 LRQIEKDItafLKKIIADHRE--TLDPANP-----RDFIDMYLLHIEEEQK----NNAESSFNEDYLfyiigDLFIAGTD 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1095 NSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHR-PS-REETGLPFQEpakisldpdelfrscpllkASFYETMRLDS- 1171
Cdd:cd20666    243 TTTNTLLWCLLYMSLYPEVQEKVQAEIDTVIGPDRaPSlTDKAQMPFTE-------------------ATIMEVQRMTVv 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1172 AGLSFREVTSDLTVTespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdpDTGAQKADMH 1251
Cdd:cd20666    304 VPLSIPHMASENTVL--------------QGYTIPKGTVIVPNLWSVHRDPAIWEKPDDFMPSRFL----DENGQLIKKE 365
                          330       340
                   ....*....|....*....|....*
gi 1834010771 1252 TIYPFGGGVSGCKGRALAERTILLF 1276
Cdd:cd20666    366 AFIPFGIGRRVCMGEQLAKMELFLM 390
RRM smart00360
RNA recognition motif;
202-257 1.70e-05

RNA recognition motif;


Pssm-ID: 214636 [Multi-domain]  Cd Length: 73  Bit Score: 44.51  E-value: 1.70e-05
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771   202 DLNTETLYTLFRPYGKIRDIE-KQPSDSKVTPRYAFVEFSRPKYAGMAKNCMHGFTV 257
Cdd:smart00360   10 DTTEEELRELFSKFGKVESVRlVRDKETGKSKGFAFVEFESEEDAEKALEALNGKEL 66
CYP71_clan cd20618
Plant cytochrome P450s, clan CYP71; The number of cytochrome P450s (P450s, CYPs) in plants is ...
1157-1293 2.21e-05

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: 49.09  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDSAG-LSF-REVTSDLTVTEspedaaaanlgdprtYRIKKGGNI-IMAHGVvQRDPQLFSNPEQFDP 1233
Cdd:cd20618    289 PYLQAVVKETLRLHPPGpLLLpHESTEDCKVAG---------------YDIPAGTRVlVNVWAI-GRDPKVWEDPLEFKP 352
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1834010771 1234 LRFIVTDPDTgAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIISM--WDIEPASGKE 1293
Cdd:cd20618    353 ERFLESDIDD-VKGQDFELL-PFGSGRRMCPGMPLGLRMVQLTLANLLHGfdWSLPGPKPED 412
CYP59-like cd11051
cytochrome P450 family 59 and similar cytochrome P450s; This family is composed of Aspergillus ...
1148-1289 2.86e-05

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: 48.79  E-value: 2.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1148 DPDELFRSCPLLKASFYETMRLDSAGLSFREVTSDLTVTESpedaaaaNLGDPRTYrikkGGNIIMAHGVVQRDPQLFSN 1227
Cdd:cd11051    243 EGPELLNQLPYTTAVIKETLRLFPPAGTARRGPPGVGLTDR-------DGKEYPTD----GCIVYVCHHAIHRDPEYWPR 311
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1834010771 1228 PEQFDPLRFIVTDPdtgaqkadmHTIY-------PFGGGVSGCKGRALAERTILLFSAAIISMWDIEPA 1289
Cdd:cd11051    312 PDEFIPERWLVDEG---------HELYppksawrPFERGPRNCIGQELAMLELKIILAMTVRRFDFEKA 371
CYP26A1 cd20638
cytochrome P450 family 26, subfamily A, polypeptide 1; Cytochrome P450s 26A1 (CYP26A1) is a ...
1203-1291 5.87e-05

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: 47.89  E-value: 5.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMA----HGVVQrdpqLFSNPEQFDPLRFIVTDPDTGAQkadmHTIYPFGGGVSGCKGRALAERTILLFSA 1278
Cdd:cd20638    328 YQIPKGWNVIYSicdtHDVAD----IFPNKDEFNPDRFMSPLPEDSSR----FSFIPFGGGSRSCVGKEFAKVLLKIFTV 399
                           90
                   ....*....|...
gi 1834010771 1279 AIISMWDIEPASG 1291
Cdd:cd20638    400 ELARHCDWQLLNG 412
CYP2C-like cd20665
cytochrome P450 family 2, subfamily C, and similar cytochrome P450s; This CYP2C-like group ...
1201-1281 7.82e-05

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: 47.26  E-value: 7.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1201 RTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADmhtiY--PFGGGVSGCKGRALAERTILLFSA 1278
Cdd:cd20665    317 RNYLIPKGTTVITSLTSVLHDDKEFPNPEKFDPGHFL--DENGNFKKSD----YfmPFSAGKRICAGEGLARMELFLFLT 390

                   ...
gi 1834010771 1279 AII 1281
Cdd:cd20665    391 TIL 393
CYP_PhacA-like cd11066
fungal cytochrome P450s similar to Aspergillus nidulans phenylacetate 2-hydroxylase; This ...
1205-1293 8.00e-05

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: 47.31  E-value: 8.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1205 IKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADMHtiYPFGGGVSGCKGRALAERTILLFSAAIISMW 1284
Cdd:cd11066    327 IPAGTILFMNAWAANHDPEHFGDPDEFIPERWL--DASGDLIPGPPH--FSFGAGSRMCAGSHLANRELYTAICRLILLF 402

                   ....*....
gi 1834010771 1285 DIEPASGKE 1293
Cdd:cd11066    403 RIGPKDEEE 411
CYP4V-like cd20660
cytochrome P450 family 4, subfamily V, and similar cytochrome P450s; This group is composed of ...
1203-1304 9.77e-05

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: 46.87  E-value: 9.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdPDTGAQKADMHTIyPFGGGVSGCKGRALA---ERTILlfsAA 1279
Cdd:cd20660    325 YTIPKGTTVLVLTYALHRDPRQFPDPEKFDPDRFL---PENSAGRHPYAYI-PFSAGPRNCIGQKFAlmeEKVVL---SS 397
                           90       100
                   ....*....|....*....|....*....
gi 1834010771 1280 IISMWDIEPASGKEFAIP-GH---RPSSG 1304
Cdd:cd20660    398 ILRNFRIESVQKREDLKPaGElilRPVDG 426
PLN02987 PLN02987
Cytochrome P450, family 90, subfamily A
1153-1289 1.17e-04

Cytochrome P450, family 90, subfamily A


Pssm-ID: 166628 [Multi-domain]  Cd Length: 472  Bit Score: 46.90  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1153 FRSCPLLKASFYETMRL-DSAGLSFREVTSDLTVtespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQF 1231
Cdd:PLN02987   326 YKSMPFTQCVVNETLRVaNIIGGIFRRAMTDIEV---------------KGYTIPKGWKVFASFRAVHLDHEYFKDARTF 390
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1834010771 1232 DPLRFIVTDPDTGAqkADMHTiyPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPA 1289
Cdd:PLN02987   391 NPWRWQSNSGTTVP--SNVFT--PFGGGPRLCPGYELARVALSVFLHRLVTRFSWVPA 444
CYP19A1 cd20616
cytochrome P450 family 19, subfamily A, polypeptide 1; CYP19A1, also called aromatase or ...
1164-1269 1.26e-04

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: 46.58  E-value: 1.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1164 YETMRldsaglsFREVTsDLTVTESPEDAAAANlgdprtYRIKKGGNIIMAHGVVQRDPqLFSNPEQFDPLRFIVTDPDT 1243
Cdd:cd20616    290 NESMR-------YQPVV-DFVMRKALEDDVIDG------YPVKKGTNIILNIGRMHRLE-FFPKPNEFTLENFEKNVPSR 354
                           90       100
                   ....*....|....*....|....*.
gi 1834010771 1244 GAQkadmhtiyPFGGGVSGCKGRALA 1269
Cdd:cd20616    355 YFQ--------PFGFGPRSCVGKYIA 372
CYP3A cd20650
cytochrome P450 family 3, subfamily A; The cytochrome P450 3A (CYP3A) subfamily, the most ...
1205-1312 1.48e-04

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: 46.25  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1205 IKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTgaqkADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMW 1284
Cdd:cd20650    322 IPKGTVVMIPTYALHRDPQYWPEPEEFRPERFSKKNKDN----IDPYIYLPFGSGPRNCIGMRFALMNMKLALVRVLQNF 397
                           90       100
                   ....*....|....*....|....*...
gi 1834010771 1285 DIEPAsgKEFAIPGHRPSSGAYLPKNDI 1312
Cdd:cd20650    398 SFKPC--KETQIPLKLSLQGLLQPEKPI 423
CYP93 cd20655
cytochrome P450 family 93; The cytochrome P450 family 93 (CYP93) is specifically found in ...
1157-1281 1.81e-04

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: 46.05  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDSAG-LSFREVTSDLTVtespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLR 1235
Cdd:cd20655    288 PYLQAVVKETLRLHPPGpLLVRESTEGCKI---------------NGYDIPEKTTLFVNVYAIMRDPNYWEDPLEFKPER 352
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1834010771 1236 FIVTDPDTGA-QKADMHTIY-PFGGGVSGCKGRALAERTILLFSAAII 1281
Cdd:cd20655    353 FLASSRSGQElDVRGQHFKLlPFGSGRRGCPGASLAYQVVGTAIAAMV 400
PLN02394 PLN02394
trans-cinnamate 4-monooxygenase
1102-1293 2.02e-04

trans-cinnamate 4-monooxygenase


Pssm-ID: 215221 [Multi-domain]  Cd Length: 503  Bit Score: 46.26  E-value: 2.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1102 WHILRIYSDPALLEEIRKEIAPFANAhrpsreetGLPFQEPakislDPDELfrscPLLKASFYETMRLDSAglsfrevts 1181
Cdd:PLN02394   315 WGIAELVNHPEIQKKLRDELDTVLGP--------GNQVTEP-----DTHKL----PYLQAVVKETLRLHMA--------- 368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1182 dltvteSPEDAAAANLGDPRT--YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKADMHTIyPFGGG 1259
Cdd:PLN02394   369 ------IPLLVPHMNLEDAKLggYDIPAESKILVNAWWLANNPELWKNPEEFRPERFLEEEAKVEANGNDFRFL-PFGVG 441
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1834010771 1260 VSGCKGRALAERTILLFSAAIISMWDIEPASGKE 1293
Cdd:PLN02394   442 RRSCPGIILALPILGIVLGRLVQNFELLPPPGQS 475
CYP2G cd20670
cytochrome P450 family 2, subfamily G; CYP2G1 is uniquely expressed in the olfactory mucosa of ...
1201-1288 2.51e-04

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: 45.69  E-value: 2.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1201 RTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdpDTGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAI 1280
Cdd:cd20670    317 RGYLLPKGTDVFPLLGSVLKDPKYFRYPEAFYPQHFL----DEQGRFKKNEAFVPFSSGKRVCLGEAMARMELFLYFTSI 392

                   ....*...
gi 1834010771 1281 ISMWDIEP 1288
Cdd:cd20670    393 LQNFSLRS 400
CYP2R1 cd20661
cytochrome P450 2R1; CYP2R1, also called vitamin D 25-hydroxylase (EC 1.14.14.24), is a ...
1099-1307 2.62e-04

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: 45.58  E-value: 2.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1099 VVFWHILRIYSDPALLEEIRKEIAPFANAHRPSReetglpFQEPAKIsldpdelfrscPLLKASFYETMRL-DSAGLS-F 1176
Cdd:cd20661    257 VLRWAILFMALYPNIQGQVQKEIDLVVGPNGMPS------FEDKCKM-----------PYTEAVLHEVLRFcNIVPLGiF 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1177 REVTSDLTVtespedaaaanlgdpRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdpDTGAQKADMHTIYPF 1256
Cdd:cd20661    320 HATSKDAVV---------------RGYSIPKGTTVITNLYSVHFDEKYWSDPEVFHPERFL----DSNGQFAKKEAFVPF 380
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1834010771 1257 GGGVSGCKGRALAERTILLFSAAIISMWDIEPASGkefAIPGHRPSSGAYL 1307
Cdd:cd20661    381 SLGRRHCLGEQLARMEMFLFFTALLQRFHLHFPHG---LIPDLKPKLGMTL 428
CYP2A cd20668
cytochrome P450 family 2, subfamily A; Cytochrome P450 family 2, subfamily A (CYP2A) includes ...
1201-1281 3.07e-04

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: 45.56  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1201 RTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtdpDTGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAI 1280
Cdd:cd20668    317 RDFFLPKGTEVFPMLGSVLKDPKFFSNPKDFNPQHFL----DDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFFTTI 392

                   .
gi 1834010771 1281 I 1281
Cdd:cd20668    393 M 393
CYP2 cd11026
cytochrome P450 family 2; The cytochrome P450 family 2 (CYP2 or Cyp2) is one of the largest, ...
1201-1280 4.50e-04

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: 44.86  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1201 RTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIvtDPDTGAQKADMHtiYPFGGGVSGCKGRALAERTILLFSAAI 1280
Cdd:cd11026    317 RGYTIPKGTTVIPNLTSVLRDPKQWETPEEFNPGHFL--DEQGKFKKNEAF--MPFSAGKRVCLGEGLARMELFLFFTSL 392
CYP1B1-like cd20675
cytochrome P450 family 1, subfamily B, polypeptide 1 and similar cytochrome P450s; Cytochrome ...
1157-1278 4.68e-04

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: 44.99  E-value: 4.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLDSaglsFREVT------SDLTVtespedaaaanLGdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQ 1230
Cdd:cd20675    295 PYVMAFLYEAMRFSS----FVPVTiphattADTSI-----------LG----YHIPKDTVVFVNQWSVNHDPQKWPNPEV 355
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1834010771 1231 FDPLRFIvtDPDTGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSA 1278
Cdd:cd20675    356 FDPTRFL--DENGFLNKDLASSVMIFSVGKRRCIGEELSKMQLFLFTS 401
CYP27C1 cd20647
cytochrome P450 family 27, subfamily C, polypeptide 1, also called all-trans retinol 3, ...
1157-1312 4.91e-04

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: 44.91  E-value: 4.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLdsaglsFREVTSDLTVTEspEDAAAANlgdprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRF 1236
Cdd:cd20647    297 PLIRALLKETLRL------FPVLPGNGRVTQ--DDLIVGG------YLIPKGTQLALCHYSTSYDEENFPRAEEFRPERW 362
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834010771 1237 IVTDpdtGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKEfaiPGHRPSSGAYLPKNDI 1312
Cdd:cd20647    363 LRKD---ALDRVDNFGSIPFGYGIRSCIGRRIAELEIHLALIQLLQNFEIKVSPQTT---EVHAKTHGLLCPGGSI 432
PLN02648 PLN02648
allene oxide synthase
1157-1237 6.05e-04

allene oxide synthase


Pssm-ID: 215350  Cd Length: 480  Bit Score: 44.54  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1157 PLLKASFYETMRLD-SAGLSFREVTSDLTVtESpEDAAaanlgdprtYRIKKGGniiMAHG---VVQRDPQLFSNPEQFD 1232
Cdd:PLN02648   334 PLVKSVVYEALRIEpPVPFQYGRAREDFVI-ES-HDAA---------FEIKKGE---MLFGyqpLVTRDPKVFDRPEEFV 399

                   ....*
gi 1834010771 1233 PLRFI 1237
Cdd:PLN02648   400 PDRFM 404
CYP4B_4F-like cd20659
cytochrome P450 family 4, subfamilies B and F, and similar cytochrome P450s; This group is ...
1165-1313 7.16e-04

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: 44.08  E-value: 7.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDS-AGLSFREVTSDLTVtespedaaaanlgDPRTyrIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDT 1243
Cdd:cd20659    295 ESLRLYPpVPFIARTLTKPITI-------------DGVT--LPAGTLIAINIYALHHNPTVWEDPEEFDPERF---LPEN 356
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1834010771 1244 gAQKADMHTIYPFGGGVSGCKGRALA---ERTILlfsAAIISMWDIEPASGKEFaipghRPSSGAYL-PKNDIK 1313
Cdd:cd20659    357 -IKKRDPFAFIPFSAGPRNCIGQNFAmneMKVVL---ARILRRFELSVDPNHPV-----EPKPGLVLrSKNGIK 421
CYP98 cd20656
cytochrome P450 family 98; Cytochrome P450 family 98 (CYP98) monooxygenases catalyze the ...
1203-1268 1.06e-03

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: 43.63  E-value: 1.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTgaqKADMHTIYPFGGGVSGCKGRAL 1268
Cdd:cd20656    323 YDIPKGANVHVNVWAIARDPAVWKNPLEFRPERFLEEDVDI---KGHDFRLLPFGAGRRVCPGAQL 385
CYP21 cd20674
cytochrome P450 21, also called steroid 21-hydroxylase; Cytochrome P450 21 (CYP21 or Cyp21), ...
1203-1308 1.25e-03

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: 43.56  E-value: 1.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGG----NIIMAHgvvqRDPQLFSNPEQFDPLRFIvtDPDTGAQKadmhtIYPFGGGVSGCKGRALAERTILLFSA 1278
Cdd:cd20674    319 YDIPKGTvvipNLQGAH----LDETVWEQPHEFRPERFL--EPGAANRA-----LLPFGCGARVCLGEPLARLELFVFLA 387
                           90       100       110
                   ....*....|....*....|....*....|
gi 1834010771 1279 AIISMWDIEPASGKefAIPGHRPSSGAYLP 1308
Cdd:cd20674    388 RLLQAFTLLPPSDG--ALPSLQPVAGINLK 415
PLN02738 PLN02738
carotene beta-ring hydroxylase
1203-1291 1.32e-03

carotene beta-ring hydroxylase


Pssm-ID: 215393 [Multi-domain]  Cd Length: 633  Bit Score: 43.75  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDTGAQKADMHTIyPFGGGVSGCKGRALAERTILLFSAAIIS 1282
Cdd:PLN02738   482 YPIKRGEDIFISVWNLHRSPKHWDDAEKFNPERWPLDGPNPNETNQNFSYL-PFGGGPRKCVGDMFASFENVVATAMLVR 560

                   ....*....
gi 1834010771 1283 MWDIEPASG 1291
Cdd:PLN02738   561 RFDFQLAPG 569
CYP46A1-like cd20613
cytochrome P450 family 46, subfamily A, polypeptide 1, also called cholesterol 24-hydroxylase, ...
1165-1304 1.34e-03

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: 43.28  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDS-AGLSFREVTSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPDt 1243
Cdd:cd20613    302 ETLRLYPpVPGTSRELTKDIE------------LGG---YKIPAGTTVLVSTYVMGRMEEYFEDPLKFDPERFSPEAPE- 365
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1244 gaqKADMHTIYPFGGGVSGCKGRALAE---RTILlfsAAIISMWDIEPASGKEFAIPGH---RPSSG 1304
Cdd:cd20613    366 ---KIPSYAYFPFSLGPRSCIGQQFAQieaKVIL---AKLLQNFKFELVPGQSFGILEEvtlRPKDG 426
CYP199A2-like cd11037
cytochrome P450 family 199, subfamily A, polypeptide 2 and similar cytochrome P450s; This ...
1149-1269 1.45e-03

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: 42.96  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1149 PD--ELFRSCP-LLKASFYETMRLDSAGLSF-REVTSDltvTEspedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQL 1224
Cdd:cd11037    233 PDqwERLRADPsLAPNAFEEAVRLESPVQTFsRTTTRD---TE---------LAG---VTIPAGSRVLVFLGSANRDPRK 297
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1834010771 1225 FSNPEQFDPLRfivtdpdtgaqKADMHTiyPFGGGVSGCKGRALA 1269
Cdd:cd11037    298 WDDPDRFDITR-----------NPSGHV--GFGHGVHACVGQHLA 329
P450_epoK-like cd20630
cytochrome P450epok and similar cytochrome P450s; Sorangium cellulosum cytochrome P450epoK is ...
1158-1276 2.44e-03

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: 42.41  E-value: 2.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1158 LLKASFYETMRLDSAGLSFrevtsdlTVTESPEDAAAAnlGDPrtyrIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRfi 1237
Cdd:cd20630    246 LLRNALEEVLRWDNFGKMG-------TARYATEDVELC--GVT----IRKGQMVLLLLPSALRDEKVFSDPDRFDVRR-- 310
                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1834010771 1238 vtdpDTGAQKAdmhtiypFGGGVSGCKGRALAERTILLF 1276
Cdd:cd20630    311 ----DPNANIA-------FGYGPHFCIGAALARLELELA 338
RRM_PPIE cd12347
RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This ...
200-253 2.56e-03

RNA recognition motif (RRM) found in cyclophilin-33 (Cyp33) and similar proteins; This subfamily corresponds to the RRM of Cyp33, also termed peptidyl-prolyl cis-trans isomerase E (PPIase E), or cyclophilin E, or rotamase E. Cyp33 is a nuclear RNA-binding cyclophilin with an N-terminal RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain), and a C-terminal PPIase domain. Cyp33 possesses RNA-binding activity and preferentially binds to polyribonucleotide polyA and polyU, but hardly to polyG and polyC. It binds specifically to mRNA, which can stimulate its PPIase activity. Moreover, Cyp33 interacts with the third plant homeodomain (PHD3) zinc finger cassette of the mixed lineage leukemia (MLL) proto-oncoprotein and a poly-A RNA sequence through its RRM domain. It further mediates downregulation of the expression of MLL target genes HOXC8, HOXA9, CDKN1B, and C-MYC, in a proline isomerase-dependent manner. Cyp33 also possesses a PPIase activity that catalyzes cis-trans isomerization of the peptide bond preceding a proline, which has been implicated in the stimulation of folding and conformational changes in folded and unfolded proteins. The PPIase activity can be inhibited by the immunosuppressive drug cyclosporin A.


Pssm-ID: 409783 [Multi-domain]  Cd Length: 75  Bit Score: 38.36  E-value: 2.56e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1834010771  200 AADLNTETLYTLFRPYGKIRDIEkQPSDSKVTPR--YAFVEFSRPKYAGMAKNCMH 253
Cdd:cd12347      7 AEEVDEKVLHAAFIPFGDIVDIQ-IPLDYETEKHrgFAFVEFEEAEDAAAAIDNMN 61
CYP81 cd20653
cytochrome P450 family 81; The only characterized member of the cytochrome P450 family 81 ...
1156-1293 2.92e-03

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: 42.21  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1156 CPLLKASFYETMRLDSAG--LSFREVTSDLTVTEspedaaaanlgdprtYRIKKGgNIIMAHG-VVQRDPQLFSNPEQFD 1232
Cdd:cd20653    286 LPYLQNIISETLRLYPAAplLVPHESSEDCKIGG---------------YDIPRG-TMLLVNAwAIHRDPKLWEDPTKFK 349
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1834010771 1233 PLRFivtdpdtGAQKADMHTIYPFGGGVSGCKGRALAERTILLFSAAIISMWDIEPASGKE 1293
Cdd:cd20653    350 PERF-------EGEEREGYKLIPFGLGRRACPGAGLAQRVVGLALGSLIQCFEWERVGEEE 403
PLN02936 PLN02936
epsilon-ring hydroxylase
1086-1269 4.00e-03

epsilon-ring hydroxylase


Pssm-ID: 178524 [Multi-domain]  Cd Length: 489  Bit Score: 42.09  E-value: 4.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1086 LSLFWALNANSPTVVFWHILRIYSDPALLEEIRKEIAPFANAHRPSREETglpfqepakisldpdelfRSCPLLKASFYE 1165
Cdd:PLN02936   284 LSMLVAGHETTGSVLTWTLYLLSKNPEALRKAQEELDRVLQGRPPTYEDI------------------KELKYLTRCINE 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1166 TMRL--DSAGLSFREVTSDLTvtespedaaaanlgdPRTYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFivtDPDt 1243
Cdd:PLN02936   346 SMRLypHPPVLIRRAQVEDVL---------------PGGYKVNAGQDIMISVYNIHRSPEVWERAEEFVPERF---DLD- 406
                          170       180
                   ....*....|....*....|....*....
gi 1834010771 1244 GAQKADMHTIY---PFGGGVSGCKGRALA 1269
Cdd:PLN02936   407 GPVPNETNTDFryiPFSGGPRKCVGDQFA 435
RBD_RRM1_NPL3 cd12340
RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 3 (Npl3p) and similar proteins; ...
202-255 4.90e-03

RNA recognition motif 1 (RRM1) found in yeast nucleolar protein 3 (Npl3p) and similar proteins; This subfamily corresponds to the RRM1 of Npl3p, also termed mitochondrial targeting suppressor 1 protein, or nuclear polyadenylated RNA-binding protein 1. Npl3p is a major yeast RNA-binding protein that competes with 3'-end processing factors, such as Rna15, for binding to the nascent RNA, protecting the transcript from premature termination and coordinating transcription termination and the packaging of the fully processed transcript for export. It specifically recognizes a class of G/U-rich RNAs. Npl3p is a multi-domain protein containing two central RNA recognition motifs (RRMs), also termed RBDs (RNA binding domains) or RNPs (ribonucleoprotein domains), separated by a short linker and a C-terminal domain rich in glycine, arginine and serine residues.


Pssm-ID: 409777 [Multi-domain]  Cd Length: 69  Bit Score: 37.38  E-value: 4.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1834010771  202 DLNTETLYTLFRPYGKIRDIeKQPSDSKvtprYAFVEFSRPKYAGMAKNCMHGF 255
Cdd:cd12340     10 DTSESAIREIFSPYGPVKEV-KMLSDSN----FAFVEFEELEDAIRAKDSVHGR 58
CYP130-like cd11078
cytochrome P450 family 130-like and similar cytochrome P450s; This subfamily includes ...
1165-1269 5.46e-03

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: 41.43  E-value: 5.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDSAGLS-FREVTSDLTVtespedaaaanlGDprtYRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRfivtdPDT 1243
Cdd:cd11078    259 ETLRYDSPVQGlRRTATRDVEI------------GG---VTIPAGARVLLLFGSANRDERVFPDPDRFDIDR-----PNA 318
                           90       100
                   ....*....|....*....|....*.
gi 1834010771 1244 GAQKAdmhtiypFGGGVSGCKGRALA 1269
Cdd:cd11078    319 RKHLT-------FGHGIHFCLGAALA 337
Cyp_unk cd11079
unknown subfamily of mostly bacterial cytochrome P450s; This subfamily is composed of ...
1154-1269 6.16e-03

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


Pssm-ID: 410701 [Multi-domain]  Cd Length: 350  Bit Score: 41.19  E-value: 6.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1154 RSCP-LLKASFYETMRLDSAGLSFREVTS-DLTVTESPedaaaanlgdprtyrIKKGGNIIMAHGVVQRDPQLFSNPEQF 1231
Cdd:cd11079    221 RANPaLLPAAIDEILRLDDPFVANRRITTrDVELGGRT---------------IPAGSRVTLNWASANRDERVFGDPDEF 285
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1834010771 1232 DPLRfivtdpdtgaqKADMHTIYpfGGGVSGCKGRALA 1269
Cdd:cd11079    286 DPDR-----------HAADNLVY--GRGIHVCPGAPLA 310
P450cam-like cd11035
P450cam and similar cytochrome P450s; This family is composed of cytochrome P450s (CYPs) with ...
1165-1276 6.39e-03

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: 41.04  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1165 ETMRLDSAGLSFREVTSDLTVTESPedaaaanlgdprtyrIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRfivtdpdtg 1244
Cdd:cd11035    240 ELLRRYPLVNVARIVTRDVEFHGVQ---------------LKAGDMVLLPLALANRDPREFPDPDTVDFDR--------- 295
                           90       100       110
                   ....*....|....*....|....*....|..
gi 1834010771 1245 aqKADMHTiyPFGGGVSGCKGRALAERTILLF 1276
Cdd:cd11035    296 --KPNRHL--AFGAGPHRCLGSHLARLELRIA 323
PLN02500 PLN02500
cytochrome P450 90B1
1203-1276 6.41e-03

cytochrome P450 90B1


Pssm-ID: 215276 [Multi-domain]  Cd Length: 490  Bit Score: 41.39  E-value: 6.41e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1834010771 1203 YRIKKGGNIIMAHGVVQRDPQLFSNPEQFDPLRFIVTDPD---TGAQKADMHTIYPFGGGVSGCKGRALAERTILLF 1276
Cdd:PLN02500   376 YDIPSGWKVLPVIAAVHLDSSLYDQPQLFNPWRWQQNNNRggsSGSSSATTNNFMPFGGGPRLCAGSELAKLEMAVF 452
P450_pinF1-like cd20629
cytochrome P450-pinF1 and similar cytochrome P450s; This subfamily is composed of bacterial ...
1148-1269 8.72e-03

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: 40.75  E-value: 8.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1148 DPDELFRSC---PLLKASFYETMRLDSAGLSF-REVTSDLTvtespedaaaanLGDprtYRIKKGGNIIMAHGVVQRDPQ 1223
Cdd:cd20629    222 HPEQLERVRrdrSLIPAAIEEGLRWEPPVASVpRMALRDVE------------LDG---VTIPAGSLLDLSVGSANRDED 286
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1834010771 1224 LFSNPEQFDPLRfivtdpdtgaqkADMHTIyPFGGGVSGCKGRALA 1269
Cdd:cd20629    287 VYPDPDVFDIDR------------KPKPHL-VFGGGAHRCLGEHLA 319
CYP_AurH-like cd11038
cytochrome P450 AurH and similar cytochrome P450s; This group includes Streptomyces thioluteus ...
1204-1308 9.06e-03

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: 40.43  E-value: 9.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1834010771 1204 RIKKGGNIIMAHGVVQRDPQLfsnpeqFDPLRFivtdpDTGAQKADMHTiypFGGGVSGCKGRALAeRTILLFSAAIIS- 1282
Cdd:cd11038    289 TIPAGTVVHLCSHAANRDPRV------FDADRF-----DITAKRAPHLG---FGGGVHHCLGAFLA-RAELAEALTVLAr 353
                           90       100
                   ....*....|....*....|....*..
gi 1834010771 1283 -MWDIEPASGKEFaipghRPSSGAYLP 1308
Cdd:cd11038    354 rLPTPAIAGEPTW-----LPDSGNTGP 375
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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