|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03012 |
PLN03012 |
Camelliol C synthase |
1-755 |
0e+00 |
|
Camelliol C synthase
Pssm-ID: 166653 [Multi-domain] Cd Length: 759 Bit Score: 1106.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 1 MWKLKIAEGG--SPWLRTTNNHVGRQFWEFDPNLGTPEDLAAVEEARKSFSDNRFVQKHSADLLMRLQFSRENLISPVLP 78
Cdd:PLN03012 1 MWKLKIAEGNgdDPYLFSTNNFAGRQTWEFDPDAGSPEELAAVEEARRIFYDDRFHVKASSDLIWRMQFLKEKKFEQRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 79 QVKIEDTDDVTEEMVETTLKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGALNTVLSEQHKQEMRRYLYNHQ 158
Cdd:PLN03012 81 PAKVEDAEKITFEIATNALRKGIHFFSALQASDGHWPAENAGPLFFLPPLVFCLYITGHLDEIFTQDHRKEILRYIYCHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 159 NEDGGWGLHIEGPSTMFGSVLNYVTLRLLGEGPNDGDGDM-EKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLP 237
Cdd:PLN03012 161 KEDGGWGLHIEGHSTMFCTTLNYICMRILGEGPDGGHDNAcGRARDWILDHGGATYIPSWGKTWLSILGVFDWSGSNPMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 238 PEIWLLPYFLPIHPGRMWCHCRMVYLPMSYLYGKRFVGPITSTVLSLRKELFTVPYHEVNWNEARNLCAKEDLYYPHPLV 317
Cdd:PLN03012 241 PEFWILPSFFPIHPAKMWCYCRLVYLPMSYLYGKRFVGPISPLILQLREEIYLQPYAEINWMKARHLCAKEDAYCPHPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 318 QDILWASLHKIVEPVLMRWP-GANLREKAIRTAIEHIHYEDENTRYICIGPVNKVLNMLCCWVEDPNSEAFKLHLPRIHD 396
Cdd:PLN03012 321 QDLIWDCLYIFAEPFLACWPfNKLLREKALGLAMKHIHYEDENSRYITIGCVEKALCMLACWVEDPNGDHFKKHLLRISD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 397 FLWLAEDGMKMQGYnGSQLWDTGFAIQAILATNLVEEYGPVLEKAHSFVKNSQVLEDCPGDLNYWYRHISKGAWPFSTAD 476
Cdd:PLN03012 401 YLWIAEDGMKMQSF-GSQLWDSGFALQALLASNLSNEIPDVLRRGHDFIKNSQVGENPSGDFKNMYRHISKGAWTFSDRD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 477 HGWPISDCTAEGLKAALLLSKVPKAIVGEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELINPAETFGDIVID 556
Cdd:PLN03012 480 HGWQASDCTAEGFKCCLLFSMIAPDIVGPKMDPEQLHDAVNILLSLQSKNGGMTAWEPAGAPEWLELLNPTEMFADIVIE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 557 YPYVECTSAAIQALISFRKLYPGHRKKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTLKNSP 636
Cdd:PLN03012 560 HEYNECTSSAIQALILFKQLYPDHRTEEINAFIKKAAEYIENIQMLDGSWYGNWGICFTYGTWFALAGLAAAGKTFNDCE 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 637 HVAKACEFLLSKQQPSGGWGESYLSCQDKVYSNLDGNRSHVVNTAWAMLALIGAGQAEVDRKPLHRAARYLINAQMENGD 716
Cdd:PLN03012 640 AIRKGVHFLLAAQKDNGGWGESYLSCPKKIYIAQEGEISNLVQTAWALMGLIHAGQAERDPIPLHRAAKLIINSQLENGD 719
|
730 740 750
....*....|....*....|....*....|....*....
gi 15225650 717 FPQQEIMGVFNRNCMITYAAYRNIFPIWALGEYRCQVLL 755
Cdd:PLN03012 720 FPQQEATGAFLKNCLLHYAAYRNIFPLWALAEYRARVPL 758
|
|
| PLN02993 |
PLN02993 |
lupeol synthase |
1-759 |
0e+00 |
|
lupeol synthase
Pssm-ID: 215537 [Multi-domain] Cd Length: 763 Bit Score: 1057.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 1 MWKLKIAEGG--SPWLRTTNNHVGRQFWEFDPNLGTPEDLAAVEEARKSFSDNRFVQKHSADLLMRLQFSRENLISPVLP 78
Cdd:PLN02993 1 MWKLKIGEGNgeDPYLFSSNNFVGRQTWEFDPKAGTPEERAAVEEARRSFLDNRSRVKGCSDLLWRMQFLKEAKFEQVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 79 QVKIEDTDDVTEEMVETTLKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGALNTVLSEQHKQEMRRYLYNHQ 158
Cdd:PLN02993 81 PVKIDRGEEITYETATNALRRGVSFFSALQASDGHWPGEITGPLFFLPPLVFCLYITGHLEEVFDAEHRKEMLRHIYCHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 159 NEDGGWGLHIEGPSTMFGSVLNYVTLRLLGEGPNDGDGDM-EKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLP 237
Cdd:PLN02993 161 NEDGGWGLHIESKSVMFCTVLNYICLRMLGEGPNGGRENAcKRARQWILDHGGVTYIPSWGKFWLSILGIYDWSGTNPMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 238 PEIWLLPYFLPIHPGRMWCHCRMVYLPMSYLYGKRFVGPITSTVLSLRKELFTVPYHEVNWNEARNLCAKEDLYYPHPLV 317
Cdd:PLN02993 241 PEIWLLPSFLPIHLGKTLCYTRMVYMPMSYLYGKRFVGPITPLIMLLREELHLQPYEEINWNKARRLCAKEDMYYPHPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 318 QDILWASLHKIVEPVLMRWPGANL-REKAIRTAIEHIHYEDENTRYICIGPVNKVLNMLCCWVEDPNSEAFKLHLPRIHD 396
Cdd:PLN02993 321 QDLIWDTLHNFVEPFLTRWPLNKLvREKALQVAMKHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 397 FLWLAEDGMKMQGYnGSQLWDTGFAIQAILATNLVEEYGPVLEKAHSFVKNSQVLEDCPGDLNYWYRHISKGAWPFSTAD 476
Cdd:PLN02993 401 YMWVAEDGMKMQSF-GSQLWDTGFAIQALLASDLSDETDDVLRRGHNYIKKSQVRENPSGDFKSMYRHISKGAWTLSDRD 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 477 HGWPISDCTAEGLKAALLLSKVPKAIVGEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELINPAETFGDIVID 556
Cdd:PLN02993 480 HGWQVSDCTAEALKCCMLLSMMPADVVGQKIDPEQLYDSVNLLLSLQSENGGVTAWEPVRAYKWLELLNPTDFFANTMVE 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 557 YPYVECTSAAIQALISFRKLYPGHRKKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTLKNSP 636
Cdd:PLN02993 560 REYVECTSAVIQALVLFKQLYPDHRTKEIIKSIEKAVQFIESKQTPDGSWYGNWGICFIYATWFALGGLAAAGKTYNDCL 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 637 HVAKACEFLLSKQQPSGGWGESYLSCQDKVYSNLDGNRSHVVNTAWAMLALIGAGQAEVDRKPLHRAARYLINAQMENGD 716
Cdd:PLN02993 640 AMRKGVHFLLTIQRDDGGWGESYLSCPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDLIPLHRAAKLIITSQLENGD 719
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 15225650 717 FPQQEIMGVFNRNCMITYAAYRNIFPIWALGEYRCQVLLQQGE 759
Cdd:PLN02993 720 FPQQEILGAFMNTCMLHYATYRNTFPLWALAEYRKAAFITHAD 762
|
|
| SQCY_1 |
cd02892 |
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ... |
97-749 |
0e+00 |
|
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.
Pssm-ID: 239222 [Multi-domain] Cd Length: 634 Bit Score: 1025.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 97 LKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGALNtvlSEQHKQEMRRYLYNHQNEDGGWGLHIEGPSTMFG 176
Cdd:cd02892 1 IRRALEFLLSLQAPDGHWPGELEGPLFITAEYILLLYILGIPI---DPEHRKEIARYLRNHQNPDGGWGLHHEGPSTMFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 177 SVLNYVTLRLLGEGPNDGDgdMEKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLPPEIWLLPYFLPIHPGRMWC 256
Cdd:cd02892 78 TVLNYVALRLLGVSPDDPH--MVKARNWILSHGGAARIPVWGKIWLALLGVYPWEGVPPLPPELWLLPSWLPFHPYKFWC 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 257 HCRMVYLPMSYLYGKRFVGPITSTVLSLRKELFTVPYHEVNWNEARNlcakeDLYYPHPLVQDILWASLHkiVEPVLMRW 336
Cdd:cd02892 156 WARTVYVPMSYLYGKRPVAPITPLVLSLRDELYVEPYEKINWYKHRN-----DLYDYRPPWQRLFDALDR--LLHWYEPL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 337 PGANLREKAIRTAIEHIHYEDENTRYICIGPVNKVLNMLCCWVED-PNSEAFKLHLPRIHDFLWLAEDGMKMQGYNGSQL 415
Cdd:cd02892 229 PPKPLRRKALRKAYEWILYRDENTGYLGIIPPPKANNMLALWVLGyPDSPAFKRHLERIDDFLWLGPEGMKMCQTNGSQV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 416 WDTGFAIQAILATNLVEEYGPVLEKAHSFVKNSQVlEDCPGDLNYWYRHISKGAWPFSTADHGWPISDCTAEGLKAALLL 495
Cdd:cd02892 309 WDTALAVQALLEAGLAPEFDPALKKALDWLLESQI-LDNPGDWKVKYRHLRKGGWAFSTANQGYPDSDDTAEALKALLRL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 496 SKVPKAivGEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELINPAETFGDIVIDYPYVECTSAAIQALISFRK 575
Cdd:cd02892 388 QELPPF--GEKVSRERLYDAVDWLLGMQNSNGGFAAFEPDNTYHWLENLNPFEDFGDIMIDPPYVECTGSVLEALGLFGK 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 576 LYPGHRkKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTLKNSPHVAKACEFLLSKQQPSGGW 655
Cdd:cd02892 466 LYPGHR-REIDPAIRRAVKYLLREQEPDGSWYGRWGVCYIYGTWFALEALAAAGEDYENSPYIRKACDFLLSKQNPDGGW 544
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 656 GESYLSCQDKVYsnLDGNRSHVVNTAWAMLALIGAGQAevDRKPLHRAARYLINAQMENGDFPQQEIMGVFNRNCMITYA 735
Cdd:cd02892 545 GESYLSYEDKSY--AGGGRSTVVQTAWALLALMAAGEP--DSEAVERGIKYLLNTQLPDGDWPQEEITGVGFPNFYIRYH 620
|
650
....*....|....
gi 15225650 736 AYRNIFPIWALGEY 749
Cdd:cd02892 621 NYRNYFPLWALGRY 634
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
96-750 |
0e+00 |
|
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 810.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 96 TLKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGalnTVLSEqHKQEMRRYLYNHQNEDGGWGLHIEGPSTMF 175
Cdd:TIGR01787 1 TARRAVEFLLSLQAPDGYWWGELEGPLTLLAEYVLLCHIAD---TPLPG-YREKIVRYLRHHQNEDGGWGLHIGGKSTVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 176 GSVLNYVTLRLLGEGPndGDGDMEKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLPPEIWLLPYFLPIHPGRMW 255
Cdd:TIGR01787 77 GTVLAYVALKILGMSP--DDPAMVRARNFILKQGGAVASPVFTKFWLALLGVYPWEGVPPLPPEIMLLPKWLPIHPSKSW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 256 CHCRMVYLPMSYLYGKRFVGPITStvlslRKELFTVPyheVNWNEARNLCAKEDLYYPHPLVQDILWASLHKIVEPVLMR 335
Cdd:TIGR01787 155 CRCRMVYLPMSYCYGERLSAPIDP-----REELYVED---DSIRAQRNNVAKEDLYTPHSWLLRALYGLLNLFYHPFLRK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 336 WpganLREKAIRTAIEHIHYEDentryiCIGPVNKVLNMLCCWVED-PNSEAFKLHLPRIHDFLWLAEDGMKMQGYnGSQ 414
Cdd:TIGR01787 227 A----LRKRALQWLYEHIAADG------SIGPISKAMAMLALWFLDgPNSPAFQKHLQRIDDYLWLQLDGMKMQGT-GSQ 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 415 LWDTGFAIQAILATNLV--EEYGPVLEKAHSFVKNSQVLEDCPGDLNYwYRHISK-GAWPFSTADHGWPI-SDCTAEGLK 490
Cdd:TIGR01787 296 VWDTAFAIQALRESGDHrlPEFHPALVKAHEWLLLSQIPDNPPGDWKV-YRHNLKpGGWAFSFLNCGYPDvDDTAVVALK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 491 AALLLSKVpkaivgEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELINPAETFGDIVIDYPYVECTSAAIQAL 570
Cdd:TIGR01787 375 AVLLLQED------EHVKRDRLRDAVNWILGMQSSNGGFAAYDPDNTGEWLELLNPSEVFGDIMIDPPYVDVTARVIQAL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 571 ISFrklypGHRKKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTLKNSPHVAKACEFLLSKQQ 650
Cdd:TIGR01787 449 GAF-----GHRADEIRNVLERALEYLRREQRADGSWFGRWGVNYTYGTGFVLSALAAAGRTYRNCPEVQKACDWLLSRQM 523
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 651 PSGGWGESYLSCQDKVYSNLDGnrSHVVNTAWAMLALIGAGQAevDRKPLHRAARYLINAQMENGDFPQQEIMGVFN-RN 729
Cdd:TIGR01787 524 PDGGWGEDCFSYEDPSYVGSGG--STPSQTGWALMALIAAGEA--DSEAIERGVKYLLETQRPDGDWPQEYITGVGFpKN 599
|
650 660
....*....|....*....|.
gi 15225650 730 CMITYAAYRNIFPIWALGEYR 750
Cdd:TIGR01787 600 FYLKYTNYRNIFPLWALGRYR 620
|
|
| osq_cycl |
TIGR03463 |
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ... |
106-749 |
0e+00 |
|
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella aurantiaca which produces cycloartenol, and Gemmata obscuriglobus and Methylococcus capsulatus, which each produce the closely related sterol, lanosterol.
Pssm-ID: 274591 [Multi-domain] Cd Length: 634 Bit Score: 613.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 106 TIQAHDGHWPGDYGGPMFLLPGLIITLSITGalNTVLSEQhKQEMRRYLYNHQNEDGGWGLHIEGPSTMFGSVLNYVTLR 185
Cdd:TIGR03463 3 ALQDSAGDWEGDMGGCQFIIAIAVAGLHVMG--RPPDAEE-RAAIIAHFELHQLADGAWGLDPEAPGQVFFSVLAYVALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 186 LLGEGPNDGDgdMEKGRDWIL-NHGGATNITSWGKMWLSVLGAFEWSGNNPLPPEIWLLPYFLPIHPGRMWCHCRMVYLP 264
Cdd:TIGR03463 80 LLGLGKDDAG--LARARAWFHaQPEGPKASGAWGKFILALLGLYEREGLNAVPPELFLLPESLPFHPSRFWCHCRLIYLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 265 MSYLYGKRFVGPITSTVL-SLRKELFTVPYHEVNWNEARNLCAKEDLYYPHPLVQdilwaslhKIVEPVLMRW---PGAN 340
Cdd:TIGR03463 158 IAWLSGRGARAPESDPLLaAIRQEIFAEGYEQVDFGAARERVAPTDLFTPISFVL--------KAANDLLAGYerlAGKA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 341 LREKAIRTAIEHIHYEDENTRYICIGPVNKVLNMLCCWVEDPNSEAFKLHLPRIHDFLWLAED-GMKMQGYNGSQLWDTG 419
Cdd:TIGR03463 230 LRARALDFAFEQILAEDEATHYICIGPINGLLNCLAIFAHDPDGPDLAAHLEGLEAWFWEDDAeGLRMNGANSNALWDTA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 420 FAIQAILAT-NLVEEYGPVLEKAHSFVKNSQVLEDCPGDLNYWyRHISKGAWPFSTADHGWPISDCTAEGLKAALLLSKV 498
Cdd:TIGR03463 310 FAVQALAALgELDEEAKHALEEAAAFIDAAQMLADLADPQEAF-RDPAKGGWCFSDGDHCWPISDCAAEALKALFALEEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 499 PKAIVGEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELINPAETFGDIVIDYPYVECTSAAIQALISFRKLYP 578
Cdd:TIGR03463 389 GDNRISEALGAARLQDAVEFILSMQNADGGFATYELQRGGKLLELLNPSDMFGQCMTDLSYVECTAACLGALAAWLKHHP 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 579 GHRKKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTlKNSPHVAKACEFLLSKQQPSGGWGES 658
Cdd:TIGR03463 469 DLPDAKIDAAIRKAEEFIRRRQLDDGSFMGFWGICFTYATFFGAKGLIAAGAE-PADMALQAAAAFLLEKQRADGAWGEH 547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 659 YLSCQDKVYsnLDGNRSHVVNTAWAMLALIGAGQAEVDrkPLHRAARYLINAQMENGDFPQQEIMGVFNRNCMITYAAYR 738
Cdd:TIGR03463 548 VESCLEARW--VEGKHGHAVMTAWALLALAAAGEAAHD--AAERGIAWLCEQQGEDGGWPPEGIAGIFFGAAAIDYDAYL 623
|
650
....*....|.
gi 15225650 739 NIFPIWALGEY 749
Cdd:TIGR03463 624 RIFPTWALARC 634
|
|
| SqhC |
COG1657 |
Terpene cyclase SqhC [Lipid transport and metabolism]; |
84-750 |
0e+00 |
|
Terpene cyclase SqhC [Lipid transport and metabolism];
Pssm-ID: 441263 [Multi-domain] Cd Length: 644 Bit Score: 575.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 84 DTDDVTEEMVETTLKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGalnTVLSEQHKQEMRRYLYNHQNEDGG 163
Cdd:COG1657 11 SASNAEDRSLLDAAIAAAQALLLQQQDDGGWWGGELEADVTIAAEYILLHHFL---GPDDEELEAKIARYLRRQQNDDGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 164 WGLHIEGPSTMFGSVLNYVTLRLLGEGPNDGDgdMEKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLPPEIWLL 243
Cdd:COG1657 88 WPLYHGGPGDLSTTVKAYFALKLLGDDPDAPH--MVRAREFILARGGAARANVFTKIWLALFGQYPWRGVPALPPEIMLL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 244 PYFLPIHPGRMWCHCRMVYLPMSYLYGKRFVGPITSTVlsLRKELFTVPYHEVnwnearnlcakeDLYYPHPlVQDILWA 323
Cdd:COG1657 166 PRWFPFHIYKFSYWARTVIVPLLILYARKPVAPLPPGV--GIDELFVEPPEQV------------DYYFPAP-RDRSPWS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 324 SLHKIVEPVL---MRWPGANLREKAIRTAIEHIHYEDE-NTRYICIGP-VNKVLNMLCCWVEDPNSEAFKLHLPRIHDFL 398
Cdd:COG1657 231 RFFLALDRLLrayERLPPKPLRRRALRKAEDWILERLEgDGGLGGIFPaMVNSLMALLALGYPPDHPVVRRALEALEKLL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 399 WLAEDGMKMQGyNGSQLWDTGFAIQAILATNlVEEYGPVLEKAHSFVKNSQVLEdcPGDlnyW---YRHISKGAWPFSTA 475
Cdd:COG1657 311 VETEDGARCQP-CVSPVWDTALAVQALQEAG-LPEDHPALERAADWLLSKQILV--KGD---WavkRPDVEPGGWAFQFA 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 476 DHGWPISDCTAEGLKAALLLSKVPKAIVGEPIDAkrlyeAVNVIISLQNADGGLATYELTRSYPWLELINPAEtFGdIVI 555
Cdd:COG1657 384 NDHYPDVDDTAVVLMALLRLRLPDEPRYREAIER-----AVEWILGMQSRDGGWGAFDKDNTKEWLNKIPFAD-HG-ALL 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 556 DYPYVECTSAAIQALISFrklypGHrkKEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTlKNS 635
Cdd:COG1657 457 DPPTADVTARCLEMLGQL-----GL--TEDHPAIRRAVAYLRREQEPDGSWFGRWGVNYIYGTWSVLTGLNAAGVD-PDD 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 636 PHVAKACEFLLSKQQPSGGWGESYLSCQDKVYSNLDgnRSHVVNTAWAMLALIGAGqaEVDRKPLHRAARYLINAQMENG 715
Cdd:COG1657 529 PAIRRAVAWLLSIQNADGGWGEDCRSYEDPRYVGLG--PSTASQTAWALLALLAAG--EADSPAVARGIAYLLSTQREDG 604
|
650 660 670
....*....|....*....|....*....|....*.
gi 15225650 716 DFPQQEIMGV-FNRNCMITYAAYRNIFPIWALGEYR 750
Cdd:COG1657 605 SWDEEYFTGTgFPRVFYLRYHLYRQYFPLWALARYR 640
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
410-749 |
4.16e-179 |
|
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.
Pssm-ID: 239219 [Multi-domain] Cd Length: 348 Bit Score: 516.00 E-value: 4.16e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 410 YNGSQLWDTGFAIQAILATNLVEEYGPVLEKAHSFVKNSQVLEDCPgDLNYWYRHISKGAWPFSTADHGWPISDCTAEGL 489
Cdd:cd02889 20 GEYSQVWDTALALQALLEAGLAPEFDPALKKALEWLLKSQIRDNPD-DWKVKYRHLRKGGWAFSTANQGYPDSDDTAEAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 490 KAALLLSKVPKAivGEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELinPAETFGDIVIDYPYVECTSAAIQA 569
Cdd:cd02889 99 KALLRLQKKPPD--GKKVSRERLYDAVDWLLSMQNSNGGFAAFEPDNTYKYLEL--IPEVDGDIMIDPPYVECTGSVLEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 570 LISFRKLYPGHRKkEVDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTlKNSPHVAKACEFLLSKQ 649
Cdd:cd02889 175 LGLFGKLYPEHRR-EIDPAIRRAVKYLEREQEPDGSWYGRWGVCFIYGTWFALEALAAAGED-ENSPYVRKACDWLLSKQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 650 QPSGGWGESYLSCQDKVYsnLDGNRSHVVNTAWAMLALIGAGQAevDRKPLHRAARYLINAQMENGDFPQQEIMGVFNRN 729
Cdd:cd02889 253 NPDGGWGESYESYEDPSY--AGGGRSTVVQTAWALLALMAAGEP--DSEAVKRGVKYLLNTQQEDGDWPQEEITGVFFKN 328
|
330 340
....*....|....*....|
gi 15225650 730 CMITYAAYRNIFPIWALGEY 749
Cdd:cd02889 329 FYIRYHNYRNYFPLWALGRY 348
|
|
| hopene_cyclase |
TIGR01507 |
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ... |
91-750 |
3.70e-63 |
|
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) biosynthesis. Squalene hopene cyclase, an integral membrane protein, directly cyclizes squalene into hopanoid products. [Fatty acid and phospholipid metabolism, Other]
Pssm-ID: 273661 [Multi-domain] Cd Length: 635 Bit Score: 222.84 E-value: 3.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 91 EMVETTLKRGLDFYSTIQAHDGHWPGDYGGPMFLLPGLIITLSITGALNTVLSEQhkqeMRRYLYNHQNEDGGWGLHIEG 170
Cdd:TIGR01507 12 ARTVEAIDRAVDYLLSCQKDEGYWWGELESNVTIEAEYVLLCHILDRVDRDRMEK----IRNYLLHEQREDGTWALYPGG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 171 PSTMFGSVLNYVTLRLLGEgPNDgDGDMEKGRDWILNHGGATNITSWGKMWLSVLGAFEWSGNNPLPPEIWLLPYFLPIH 250
Cdd:TIGR01507 88 PGDLSTTVEAYVALKYIGM-SRD-EPPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWRGVPMVPPEIMLLPKRFPFN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 251 PGRMWCHCRMVYLPMSYLYGKRFVGPITStvlSLR-KELFTVPYHevnwnearnlcaKEDLYYPH---PLVQDILWASLH 326
Cdd:TIGR01507 166 IYEFSSWARATVVPLSIVCSRKPVFPLPE---RARvPELYETDVP------------KPRRRGAKggtGWGIFDALDRAL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 327 KIVEPVLMRwpgaNLREKAIRTAIEHIHYEDENT-RYICIGP--VN-----KVLNMlccwveDPNSEAFKLHLPRIHDFL 398
Cdd:TIGR01507 231 HGYEKLSVH----PFRRAAEIRALDWLLERQAGDgSWGGIQPamFNalialKILGM------TQHDAFIKLGWEGIDLYG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 399 WLAEDGMKMQGyNGSQLWDTGFAIQAILATNLVEEYgPVLEKAHSFVKNSQVleDCPGDLNYWYRHISKGAWPFSTADHG 478
Cdd:TIGR01507 301 VELDDSWMFQA-CVSPVWDTALAVLALREAGLPADH-DALVKAGEWLLDKQI--TVPGDWAVKRPNLEPGGWAFQFDNVY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 479 WPISDCTAEgLKAALLLSKVPKaivgEPIDAKRLYEAVNVIISLQNADGGLATYELTRSYPWLELInpaeTFGDI--VID 556
Cdd:TIGR01507 377 YPDVDDTAV-VVWALNGLRLPD----ERRRRDAMTKAFRWIAGMQSSNGGWGAFDVDNTSDLLNHI----PFCDFgaVTD 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 557 YPYVECTSAAIQALISFRKLYPGHRkkevdecIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTlKNSP 636
Cdd:TIGR01507 448 PPTADVTARVLECLGSFGYDDAWPV-------IERAVEYLKREQEPDGSWFGRWGVNYLYGTGAVLSALKAVGID-TREP 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 637 HVAKACEFLLSKQQPSGGWGESYLSCQDKVYSNlDGNrSHVVNTAWAMLALIGAGQAEVDrkPLHRAARYLINAQMENGD 716
Cdd:TIGR01507 520 YIQKALAWLESHQNPDGGWGEDCRSYEDPAYAG-KGA-STASQTAWALIALIAAGRAESE--AARRGVQYLVETQRPDGG 595
|
650 660 670
....*....|....*....|....*....|....*
gi 15225650 717 FPQQEIMGV-FNRNCMITYAAYRNIFPIWALGEYR 750
Cdd:TIGR01507 596 WDEPYYTGTgFPGDFYLGYHMYRHVFPLLALARYK 630
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
396-749 |
3.37e-55 |
|
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.
Pssm-ID: 238362 [Multi-domain] Cd Length: 300 Bit Score: 191.61 E-value: 3.37e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 396 DFL--WLAEDGMKMQGYNGSQLWDTGFAIQAIL----ATNLVEEYGPVLEKAHSFVKNSQvledcpgdlnywyrhISKGA 469
Cdd:cd00688 6 KYLlrYPYGDGHWYQSLCGEQTWSTAWPLLALLlllaATGIRDKADENIEKGIQRLLSYQ---------------LSDGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 470 WPFSTAdHGWPISDCTAEGLKAALLLSKVpkaivgEPIDAKRLYEAVNVIISLQNADGGLATYEltrsypwlelinpaET 549
Cdd:cd00688 71 FSGWGG-NDYPSLWLTAYALKALLLAGDY------IAVDRIDLARALNWLLSLQNEDGGFREDG--------------PG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 550 FGDIVIDYPYVECTSAAIQALISFRKLYPghrkkevDECIEKAVKFIESIQAADGSWyGSWAVCFTYGTWFGVKGLVAVG 629
Cdd:cd00688 130 NHRIGGDESDVRLTAYALIALALLGKLDP-------DPLIEKALDYLLSCQNYDGGF-GPGGESHGYGTACAAAALALLG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 630 KTlkNSPHVAKACEFLLSKQQPSGGWGESYLscqdkvysnLDGNRSHVVNTAWAMLALIGAGQAEvDRKPLHRAARYLIN 709
Cdd:cd00688 202 DL--DSPDAKKALRWLLSRQRPDGGWGEGRD---------RTNKLSDSCYTEWAAYALLALGKLG-DLEDAEKLVKWLLS 269
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 15225650 710 AQMENGDFPQQEImgvfnrncmITYAAYRNIFPIWALGEY 749
Cdd:cd00688 270 QQNEDGGFSSKPG---------KSYDTQHTVFALLALSLY 300
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
413-750 |
3.99e-47 |
|
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the C-terminal half of the molecule.
Pssm-ID: 433057 [Multi-domain] Cd Length: 319 Bit Score: 170.21 E-value: 3.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 413 SQLWDTGFAIQAILATNlVEEYGPVLEKAHSFVKNSQVLEdcPGDLNYWYRHISKGAWPFSTADHGWPISDCTAeglKAA 492
Cdd:pfam13243 2 SPVWDTALALHALLEAG-VPADHPALVKAAQWLLDRQVLV--KGDWAVKRPDLEPGGWAFQFANDHYPDVDDTA---VVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 493 LLLSKVPKAIVGEPIDAKRlyEAVNVIISLQNADGGLATYELTRSYPWLELInpaeTFGDI--VIDYPYVECTSAAIQAL 570
Cdd:pfam13243 76 LALDRVRLPDERRRDDAIA--RGIEWILGMQSKNGGWGAFDKDNTKYYLNKI----PFADHgaLLDPPTADVTARVLEML 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 571 ISFrklypGHRKKevDECIEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTLkNSPHVAKACEFLLSKQQ 650
Cdd:pfam13243 150 GQL-----GYPDD--HPVAARALEYLKKEQEPDGSWFGRWGVNYIYGTWSVLCGLAAVGEDH-NRPYIRKAVDWLKSRQN 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 651 PSGGWGESYLSCQDkvYSNLDGNRSHVVNTAWAMLALIGAGqaEVDRKPLHRAARYLINAQMENGDFPQQEIMGV-FNRN 729
Cdd:pfam13243 222 PDGGWGEDCESYKD--PKLAGRGPSTASQTAWALLALMAAG--EVDSPAVRRGIQYLLETQKPDGTWDEPYFTGTgFPRV 297
|
330 340
....*....|....*....|.
gi 15225650 730 CMITYAAYRNIFPIWALGEYR 750
Cdd:pfam13243 298 FYLKYHGYRNYFPLWALARYR 318
|
|
| SQHop_cyclase_N |
pfam13249 |
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
148-357 |
8.54e-34 |
|
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the N-terminal domain.
Pssm-ID: 433061 [Multi-domain] Cd Length: 290 Bit Score: 131.45 E-value: 8.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 148 QEMRRYLYNHQNEDGGWGLHIEGPSTMFGSVLNYVTLRLLGEGPNDGDgdMEKGRDWILNHGGATNITSWGKMWLSVLGA 227
Cdd:pfam13249 48 AKIARYLRSQQREDGGWPLFHGGPGDLSTTVEAYFALKLLGDSPDAPH--MVRAREFILARGGAAKANVFTRIWLALFGQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 228 FEWSGNNPLPPEIWLLPYFLPIHPGRMWCHCRMVYLPMSYLYGKRFVGPITSTVlsLRKELFTVPYHEVNwnearnlcak 307
Cdd:pfam13249 126 YPWRGVPSMPPEIMLLPRWFPFNIYKFSSWARTTIVPLLILSALKPVAPLPPGI--GLDELFVEPPENVR---------- 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15225650 308 edlYYPHPlVQDILWASLHKIVEPVLMRWPGAN---LREKAIRTA----IEHIHYED 357
Cdd:pfam13249 194 ---YYPRP-HRLFSWTNLFLGLDRVLKLYERLPpkpLRRRALRKAeewiLERQEGDG 246
|
|
| squa_tetra_cyc |
TIGR04277 |
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, ... |
87-752 |
4.18e-23 |
|
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, occurs a small number of eukaryotes, some of them anaerobic. The pathway can occur under anaerobic conditions, and the product is thought to replace sterols, letting organisms with this compound build membrane suitable for performing phagocytosis.
Pssm-ID: 212000 [Multi-domain] Cd Length: 624 Bit Score: 104.71 E-value: 4.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 87 DVTEEMVETTLKRGLDFYstiQAHDGHW--PgDYGGPMFLLPGLIITLSITGALNTVLSEQHKQEMrryLYNHQNEDGGW 164
Cdd:TIGR04277 15 DIEEVQNAIRDAQEICWA---ELHDNEWvyP-PYLGELFISEYYFELKALGWIHKSAFEASKFTEI---LLGSQFEDGSW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 165 gLHIEGPSTMFG----SVLNYVTLRLLGEGPNDgDGDMEKGRDWILNHGGATNITSWGKMWLSVLGAFEWSgnnplppEI 240
Cdd:TIGR04277 88 -EQVEDANIETGqldaTIFNYWYLKAIGIDIHI-DAALKKAQEWIKANGGIEAAQTMTKFKLAAFGQYPWE-------DL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 241 WLLPYFLPIHPGrmwchcrmvylPMSYLYGK----RFVGPITSTVLSLRKE--LFTVPYHEVN--W-NEARNLCAKEDLY 311
Cdd:TIGR04277 159 FKIPLFIFKKKG-----------IFKPLYIKditaQWVYPHLTALAYLQNQriIFNVAVADIRelWiNKAKKGIKHQKKE 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 312 YPHPLVQDILWASLHKIVEpvlMRWPGANLREKAIRTAIEHIHYEDENTRYicigpvnkvlnmlccwvedPNseafkLHL 391
Cdd:TIGR04277 228 RPSFFIDNDLLILMDEIFK---LKQPLGSFGAYTISTLLSLLAFKDFQGKH-------------------PH-----KHK 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 392 PRIHDFLwlaEDGMKM---------QGYNGS----QLWDTgfaiqaILATNLVEEYGPVLEKAHSFVKNSqvledcpgdl 458
Cdd:TIGR04277 281 NEIQDAL---EDGLDFvefnyfnfrEAYHGSlddgRWWDT------ILISWAMLESGEDKEKIFPIVENM---------- 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 459 nywyrhISKGAWPFSTADHGW-----PISDCTAeglkaaLLLskVPKAIVGEPIdAKRLYEAVNVIISLQNADGGLATYE 533
Cdd:TIGR04277 342 ------LKEGLQPKGGIEYGYdfeyaPDADDTG------LLL--QVLSYYGEAF-ADAIDEGAEFLFSMQNDDGGFPAFD 406
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 534 LTR---------SYPWLELINPAETFgdiviDYPYVECTSAAIQALISF--RKLYPghrkkevdeCIEKAVKFIESIQAA 602
Cdd:TIGR04277 407 KGKmednllfkfAFKIAGIADSAEIF-----DPSCPDITAHILEGLGEFgdQANHD---------QIQKMIKYFMDTQEK 472
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 603 DGSWYGSWAVCFTYGTWFGVKGLVAVGKTLKNSpHVAKACEFLLSKQQPSGGWGESYLSCQDKVYSNLDGnRSHVVNTAW 682
Cdd:TIGR04277 473 FGSWEARWGINYIMAAGAVLPALAKMNYDLNEG-WAKNAINWLLNKQNADGGFGECTLSYNDPEKWNGIG-KSTVTQTSW 550
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225650 683 AMLALIGA-GQAEVDRKPLHRAARYLINA-QMENGDFPQQEIMGVFNRNCM-ITYAAYRNIFPIWALGEYRCQ 752
Cdd:TIGR04277 551 GLLALLAVeDHNDQIKEAADKAAQYLLDQfKRDDGEFKDHSTIGTGHRGLLyLQYPSYAQSFPLIALGRFLDI 623
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
589-717 |
7.57e-12 |
|
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.
Pssm-ID: 238362 [Multi-domain] Cd Length: 300 Bit Score: 66.81 E-value: 7.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 589 IEKAVKFIESIQAADGSWYGSWAVCFTYGTWFGVKGLVAVGKTL----KNSPHVAKACEFLLSKQQPSGGWGESYlscqd 664
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAATgirdKADENIEKGIQRLLSYQLSDGGFSGWG----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 15225650 665 kvysnlDGNRSHVVNTAWAMLALIGAGQAE-VDRKPLHRAARYLINAQMENGDF 717
Cdd:cd00688 76 ------GNDYPSLWLTAYALKALLLAGDYIaVDRIDLARALNWLLSLQNEDGGF 123
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
146-188 |
4.35e-10 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 55.21 E-value: 4.35e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 15225650 146 HKQEMRRYLYNHQNEDGGWGLHIEGPSTMFGSVLNYVTLRLLG 188
Cdd:pfam00432 2 DKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
507-716 |
2.15e-08 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 55.87 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 507 IDAKRLYEAVNVIISLQNADGGlatyeltrsYPWLELinpaetfgdividYPYVECTSAAIQALISFRKLYPgHRKKEVD 586
Cdd:COG5029 16 STADFTDSHLDYLRASQNPDGG---------FAGRSG-------------PSDLYSTYYAVRTLALLGESPK-WRDRVAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 587 eciekavkFIESIQAADG---SWYGSWAVcFTYGTWFGVKGLVAVGKTLknsPHVAKACEFLLSKQQPSGGWGESYlscq 663
Cdd:COG5029 73 --------LLSSLRVEDGgfaKAPEGGAG-STYHTYLATLLAELLGRPP---PDPDRLVRFLISQQNDDGGFEISP---- 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 15225650 664 dkvysnldGNRSHVVNTAWAMLALIGAGQAEVDRKplHRAARYLinAQMENGD 716
Cdd:COG5029 137 --------GRRSDTNPTAAAIGALRALGALDDPIE--TKVIRFL--RDVQSPE 177
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
587-629 |
1.01e-06 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 45.97 E-value: 1.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 15225650 587 ECIEKAVKFIESIQAADGSWYGSWAVC-FTYGTWFGVKGLVAVG 629
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGEsDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
636-691 |
1.76e-06 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 45.19 E-value: 1.76e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 15225650 636 PHVAKACEFLLSKQQPSGGWGESYLSCqdkvysnldgnrSHVVNTAWAMLALIGAG 691
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGE------------SDTYYTYCALAALALLG 44
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
638-716 |
1.30e-05 |
|
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.
Pssm-ID: 239219 [Multi-domain] Cd Length: 348 Bit Score: 47.98 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 638 VAKACEFLLSKQQPSGGWGESYlscqdkvysnldgnrSHVVNTAWAMLALIGAGQAEVDRKPLHRAARYLINAQ-MENGD 716
Cdd:cd02889 1 IRRALDFLLSLQAPDGHWPGEY---------------SQVWDTALALQALLEAGLAPEFDPALKKALEWLLKSQiRDNPD 65
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
97-208 |
4.04e-05 |
|
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.
Pssm-ID: 238362 [Multi-domain] Cd Length: 300 Bit Score: 46.39 E-value: 4.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 97 LKRGLDFYSTIQAHDGHWPGDYGGPmflLPGLIITLSITGALNTV-----LSEQHKQEMRRYLYNHQNEDGGWGLHIEGP 171
Cdd:cd00688 54 IEKGIQRLLSYQLSDGGFSGWGGND---YPSLWLTAYALKALLLAgdyiaVDRIDLARALNWLLSLQNEDGGFREDGPGN 130
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 15225650 172 STMFG-----SVLNYVTLRLLGEGPNDGDGDMEKGRDWILNH 208
Cdd:cd00688 131 HRIGGdesdvRLTAYALIALALLGKLDPDPLIEKALDYLLSC 172
|
|
| A2M_like |
cd02891 |
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
552-707 |
2.08e-04 |
|
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier protein in serum. It is a broadly specific proteinase inhibitor. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. This group contains another broadly specific proteinase inhibitor: pregnancy zone protein (PZP). PZP is a trace protein in the plasma of non-pregnant females and males which is elevated in pregnancy. Alpha (2)-M and PZ bind to placental protein-14 and may modulate its activity in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system. This group also contains C3, C4 and C5 of vertebrate complement. The vertebrate complement is an effector of both the acquired and innate immune systems The point of convergence of the classical, alternative and lectin pathways of the complement system is the proteolytic activation of C3. C4 plays a key role in propagating the classical and lectin pathways. C5 participates in the classical and alternative pathways. The thioester bond located within the structure of C3 and C4 is central to the function of complement. C5 does not contain an active thioester bond.
Pssm-ID: 239221 [Multi-domain] Cd Length: 282 Bit Score: 43.92 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 552 DIVIDYPY--VECTSAAIQALISFRKlYPGHRKKEVDECIEKAVKFIESI-------QAADGSwYGSWAVCFTYGTW--- 619
Cdd:cd02891 6 DYLLRYPYgcGEQTMSRAAPNLYVLK-YLDATGQLTPEIREKALEYIRKGyqrlltyQRSDGS-FSAWGNSDSGSTWlta 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 620 FGVKGLVAVGKTLKNSP-HVAKACEFLLSKQQPSGGWGESYlscQDKVYSNLDGNRSHVVNTAWAMLALIGAGQAevDRK 698
Cdd:cd02891 84 YVVKFLSQARKYIDVDEnVLARALGWLVPQQKEDGSFRELG---PVIHREMKGGVDDSVSLTAYVLIALAEAGKA--CDA 158
|
....*....
gi 15225650 699 PLHRAARYL 707
Cdd:cd02891 159 SIEKALAYL 167
|
|
| GGTase-II |
cd02894 |
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ... |
563-717 |
3.71e-04 |
|
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.
Pssm-ID: 239224 [Multi-domain] Cd Length: 287 Bit Score: 43.03 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 563 TSAAIQALISFRKLYpghrkkEVDECIEKAVKFIESIQAADGSWYGS-WA---VCFTYGTwfgVKGLVAVGKTlkNSPHV 638
Cdd:cd02894 82 TLSAIQILALYDLLN------KIDENKEKIAKFIKGLQNEDGSFSGDkWGevdTRFSYCA---VLCLTLLGKL--DLIDV 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 639 AKACEFLLSKQQPSGGWGESYlscqdkvysnldGNRSHV--VNTAWAMLALIGAgqaeVDRKPLHRAARYLINAQMENGD 716
Cdd:cd02894 151 DKAVDYLLSCYNFDGGFGCRP------------GAESHAgqIFCCVGALAILGS----LDLIDRDRLGWWLCERQLPSGG 214
|
.
gi 15225650 717 F 717
Cdd:cd02894 215 L 215
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
85-208 |
4.89e-04 |
|
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the C-terminal half of the molecule.
Pssm-ID: 433057 [Multi-domain] Cd Length: 319 Bit Score: 43.09 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225650 85 TDDVTEEMVET-----------TLKRGLDFYSTIQAHDGHWPGDYG-----GpmfllpgliiTLSITGALNTVlSEQHKQ 148
Cdd:pfam13243 138 TADVTARVLEMlgqlgypddhpVAARALEYLKKEQEPDGSWFGRWGvnyiyG----------TWSVLCGLAAV-GEDHNR 206
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225650 149 EMRR----YLYNHQNEDGGWG----------LHIEGPSTmfGSVLNYVTLRLLGEGpnDGDGD-MEKGRDWILNH 208
Cdd:pfam13243 207 PYIRkavdWLKSRQNPDGGWGedcesykdpkLAGRGPST--ASQTAWALLALMAAG--EVDSPaVRRGIQYLLET 277
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
93-165 |
1.88e-03 |
|
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 41.66 E-value: 1.88e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225650 93 VETTLKRGLDFYSTIQAHDGHWPGDYG-----GPMFLLPGLiitlsiTGALNTVLSEQHKQEMRRYLYNHQNEDGGWG 165
Cdd:TIGR01787 458 IRNVLERALEYLRREQRADGSWFGRWGvnytyGTGFVLSAL------AAAGRTYRNCPEVQKACDWLLSRQMPDGGWG 529
|
|
| |
