|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02993 |
PLN02993 |
lupeol synthase |
1-763 |
0e+00 |
|
lupeol synthase
Pssm-ID: 215537 [Multi-domain] Cd Length: 763 Bit Score: 1685.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 1 MWKLKIGEGNGEDPYLFSSNNFVGRQTWEFDPKAGTPEERAAVEDARRNYLDNRPRVKGCSDLLWRMQFLKEAKFEQVIP 80
Cdd:PLN02993 1 MWKLKIGEGNGEDPYLFSSNNFVGRQTWEFDPKAGTPEERAAVEEARRSFLDNRSRVKGCSDLLWRMQFLKEAKFEQVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 81 PVKIDDGEGITYKNATDALRRAVSFYSALQSSDGHWPAEITGTLFFLPPLVFCFYITGHLEKIFDAEHRKEMLRHIYCHQ 160
Cdd:PLN02993 81 PVKIDRGEEITYETATNALRRGVSFFSALQASDGHWPGEITGPLFFLPPLVFCLYITGHLEEVFDAEHRKEMLRHIYCHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 161 NEDGGWGLHIEGKSVMFCTVLNYICLRMLGEGPNGGRNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMP 240
Cdd:PLN02993 161 NEDGGWGLHIESKSVMFCTVLNYICLRMLGEGPNGGRENACKRARQWILDHGGVTYIPSWGKFWLSILGIYDWSGTNPMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 241 PEIWLLPSFFPIHLGKTLCYTRMVYMPMSYLYGKRFVGPLTPLIMLLRKELHLQPYEEINWNKARRLCAKEDMIYPHPLV 320
Cdd:PLN02993 241 PEIWLLPSFLPIHLGKTLCYTRMVYMPMSYLYGKRFVGPITPLIMLLREELHLQPYEEINWNKARRLCAKEDMYYPHPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 321 QDLLWDTLHNFVEPILTNWPLKKLVREKALRVAMEHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPD 400
Cdd:PLN02993 321 QDLIWDTLHNFVEPFLTRWPLNKLVREKALQVAMKHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 401 FMWVAEDGLKMQSFGSQLWDTVFAIQALLACDLSDETDDVLRKGHSFIKKSQVRENPSGDFKSMYRHISKGAWTLSDRDH 480
Cdd:PLN02993 401 YMWVAEDGMKMQSFGSQLWDTGFAIQALLASDLSDETDDVLRRGHNYIKKSQVRENPSGDFKSMYRHISKGAWTLSDRDH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 481 GWQVSDCTAEALKCCMLLSMMPAEVVGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFFTCVMAER 560
Cdd:PLN02993 481 GWQVSDCTAEALKCCMLLSMMPADVVGQKIDPEQLYDSVNLLLSLQSENGGVTAWEPVRAYKWLELLNPTDFFANTMVER 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 561 EYVECTSAVIQALVLFKQLYPDHRTKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKSCLA 640
Cdd:PLN02993 561 EYVECTSAVIQALVLFKQLYPDHRTKEIIKSIEKAVQFIESKQTPDGSWYGNWGICFIYATWFALGGLAAAGKTYNDCLA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 641 VRKGVDFLLAIQEEDGGWGESHLSCPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDPTPLHRAAKLIITSQLENGDF 720
Cdd:PLN02993 641 MRKGVHFLLTIQRDDGGWGESYLSCPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDLIPLHRAAKLIITSQLENGDF 720
|
730 740 750 760
....*....|....*....|....*....|....*....|...
gi 30699377 721 PQQEILGVFMNTCMLHYATYRNIFPLWALAEYRKAAFATHQDL 763
Cdd:PLN02993 721 PQQEILGAFMNTCMLHYATYRNTFPLWALAEYRKAAFITHADL 763
|
|
| PLN03012 |
PLN03012 |
Camelliol C synthase |
1-754 |
0e+00 |
|
Camelliol C synthase
Pssm-ID: 166653 [Multi-domain] Cd Length: 759 Bit Score: 1422.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 1 MWKLKIGEGNGEDPYLFSSNNFVGRQTWEFDPKAGTPEERAAVEDARRNYLDNRPRVKGCSDLLWRMQFLKEAKFEQVIP 80
Cdd:PLN03012 1 MWKLKIAEGNGDDPYLFSTNNFAGRQTWEFDPDAGSPEELAAVEEARRIFYDDRFHVKASSDLIWRMQFLKEKKFEQRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 81 PVKIDDGEGITYKNATDALRRAVSFYSALQSSDGHWPAEITGTLFFLPPLVFCFYITGHLEKIFDAEHRKEMLRHIYCHQ 160
Cdd:PLN03012 81 PAKVEDAEKITFEIATNALRKGIHFFSALQASDGHWPAENAGPLFFLPPLVFCLYITGHLDEIFTQDHRKEILRYIYCHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 161 NEDGGWGLHIEGKSVMFCTVLNYICLRMLGEGPNGGRNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMP 240
Cdd:PLN03012 161 KEDGGWGLHIEGHSTMFCTTLNYICMRILGEGPDGGHDNACGRARDWILDHGGATYIPSWGKTWLSILGVFDWSGSNPMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 241 PEIWLLPSFFPIHLGKTLCYTRMVYMPMSYLYGKRFVGPLTPLIMLLRKELHLQPYEEINWNKARRLCAKEDMIYPHPLV 320
Cdd:PLN03012 241 PEFWILPSFFPIHPAKMWCYCRLVYLPMSYLYGKRFVGPISPLILQLREEIYLQPYAEINWMKARHLCAKEDAYCPHPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 321 QDLLWDTLHNFVEPILTNWPLKKLVREKALRVAMEHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPD 400
Cdd:PLN03012 321 QDLIWDCLYIFAEPFLACWPFNKLLREKALGLAMKHIHYEDENSRYITIGCVEKALCMLACWVEDPNGDHFKKHLLRISD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 401 FMWVAEDGLKMQSFGSQLWDTVFAIQALLACDLSDETDDVLRKGHSFIKKSQVRENPSGDFKSMYRHISKGAWTLSDRDH 480
Cdd:PLN03012 401 YLWIAEDGMKMQSFGSQLWDSGFALQALLASNLSNEIPDVLRRGHDFIKNSQVGENPSGDFKNMYRHISKGAWTFSDRDH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 481 GWQVSDCTAEALKCCMLLSMMPAEVVGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFFTCVMAER 560
Cdd:PLN03012 481 GWQASDCTAEGFKCCLLFSMIAPDIVGPKMDPEQLHDAVNILLSLQSKNGGMTAWEPAGAPEWLELLNPTEMFADIVIEH 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 561 EYVECTSAVIQALVLFKQLYPDHRTKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKSCLA 640
Cdd:PLN03012 561 EYNECTSSAIQALILFKQLYPDHRTEEINAFIKKAAEYIENIQMLDGSWYGNWGICFTYGTWFALAGLAAAGKTFNDCEA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 641 VRKGVDFLLAIQEEDGGWGESHLSCPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDPTPLHRAAKLIITSQLENGDF 720
Cdd:PLN03012 641 IRKGVHFLLAAQKDNGGWGESYLSCPKKIYIAQEGEISNLVQTAWALMGLIHAGQAERDPIPLHRAAKLIINSQLENGDF 720
|
730 740 750
....*....|....*....|....*....|....
gi 30699377 721 PQQEILGVFMNTCMLHYATYRNIFPLWALAEYRK 754
Cdd:PLN03012 721 PQQEATGAFLKNCLLHYAAYRNIFPLWALAEYRA 754
|
|
| SQCY_1 |
cd02892 |
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ... |
99-752 |
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: 950.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 99 LRRAVSFYSALQSSDGHWPAEITGTLFFLPPLVFCFYITGHlekIFDAEHRKEMLRHIYCHQNEDGGWGLHIEGKSVMFC 178
Cdd:cd02892 1 IRRALEFLLSLQAPDGHWPGELEGPLFITAEYILLLYILGI---PIDPEHRKEIARYLRNHQNPDGGWGLHHEGPSTMFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 179 TVLNYICLRMLGEGPNGGrnnACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLLPSFFPIHLGKTL 258
Cdd:cd02892 78 TVLNYVALRLLGVSPDDP---HMVKARNWILSHGGAARIPVWGKIWLALLGVYPWEGVPPLPPELWLLPSWLPFHPYKFW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 259 CYTRMVYMPMSYLYGKRFVGPLTPLIMLLRKELHLQPYEEINWNKARRlcAKEDMIYPHPLVQDLLWDTLHnFVEPILTN 338
Cdd:cd02892 155 CWARTVYVPMSYLYGKRPVAPITPLVLSLRDELYVEPYEKINWYKHRN--DLYDYRPPWQRLFDALDRLLH-WYEPLPPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 339 WplkklVREKALRVAMEHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDH-FKKHLARIPDFMWVAEDGLKM-QSFGS 416
Cdd:cd02892 232 P-----LRRKALRKAYEWILYRDENTGYLGIIPPPKANNMLALWVLGYPDSPaFKRHLERIDDFLWLGPEGMKMcQTNGS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 417 QLWDTVFAIQALLACDLSDETDDVLRKGHSFIKKSQVRENPsGDFKSMYRHISKGAWTLSDRDHGWQVSDCTAEALKCCM 496
Cdd:cd02892 307 QVWDTALAVQALLEAGLAPEFDPALKKALDWLLESQILDNP-GDWKVKYRHLRKGGWAFSTANQGYPDSDDTAEALKALL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 497 LLSMMPAEvvGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFFTCVMAEREYVECTSAVIQALVLF 576
Cdd:cd02892 386 RLQELPPF--GEKVSRERLYDAVDWLLGMQNSNGGFAAFEPDNTYHWLENLNPFEDFGDIMIDPPYVECTGSVLEALGLF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 577 KQLYPDHRtKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKSCLAVRKGVDFLLAIQEEDG 656
Cdd:cd02892 464 GKLYPGHR-REIDPAIRRAVKYLLREQEPDGSWYGRWGVCYIYGTWFALEALAAAGEDYENSPYIRKACDFLLSKQNPDG 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 657 GWGESHLSCPEQRYipLEGNRSNLVQTAWAMMGLIHAGQAerDPTPLHRAAKLIITSQLENGDFPQQEILGVFMNTCMLH 736
Cdd:cd02892 543 GWGESYLSYEDKSY--AGGGRSTVVQTAWALLALMAAGEP--DSEAVERGIKYLLNTQLPDGDWPQEEITGVGFPNFYIR 618
|
650
....*....|....*.
gi 30699377 737 YATYRNIFPLWALAEY 752
Cdd:cd02892 619 YHNYRNYFPLWALGRY 634
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
98-754 |
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: 795.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 98 ALRRAVSFYSALQSSDGHWPAEITGTLFFLPPLVFCFYITGhlekIFDAEHRKEMLRHIYCHQNEDGGWGLHIEGKSVMF 177
Cdd:TIGR01787 1 TARRAVEFLLSLQAPDGYWWGELEGPLTLLAEYVLLCHIAD----TPLPGYREKIVRYLRHHQNEDGGWGLHIGGKSTVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 178 CTVLNYICLRMLGEGPNggrNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLLPSFFPIHLGKT 257
Cdd:TIGR01787 77 GTVLAYVALKILGMSPD---DPAMVRARNFILKQGGAVASPVFTKFWLALLGVYPWEGVPPLPPEIMLLPKWLPIHPSKS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 258 LCYTRMVYMPMSYLYGKRFVGPLTPlimllRKELHLQPYEEinwNKARRLCAKEDMIYPHPLVQDLLWDTLHNFVEPILT 337
Cdd:TIGR01787 154 WCRCRMVYLPMSYCYGERLSAPIDP-----REELYVEDDSI---RAQRNNVAKEDLYTPHSWLLRALYGLLNLFYHPFLR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 338 NWplkklVREKALRVAMEHIHYEDenshyiTIGCVEKVLCMLACWIEN-PNGDHFKKHLARIPDFMWVAEDGLKMQSFGS 416
Cdd:TIGR01787 226 KA-----LRKRALQWLYEHIAADG------SIGPISKAMAMLALWFLDgPNSPAFQKHLQRIDDYLWLQLDGMKMQGTGS 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 417 QLWDTVFAIQALLACDLS--DETDDVLRKGHSFIKKSQVRENPSGDFKsMYRHISK-GAWTLSDRDHGW-QVSDCTAEAL 492
Cdd:TIGR01787 295 QVWDTAFAIQALRESGDHrlPEFHPALVKAHEWLLLSQIPDNPPGDWK-VYRHNLKpGGWAFSFLNCGYpDVDDTAVVAL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 493 KCCMLLSMMpaevvgQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFFTCVMAEREYVECTSAVIQA 572
Cdd:TIGR01787 374 KAVLLLQED------EHVKRDRLRDAVNWILGMQSSNGGFAAYDPDNTGEWLELLNPSEVFGDIMIDPPYVDVTARVIQA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 573 LVLFKqlypdHRTKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKSCLAVRKGVDFLLAIQ 652
Cdd:TIGR01787 448 LGAFG-----HRADEIRNVLERALEYLRREQRADGSWFGRWGVNYTYGTGFVLSALAAAGRTYRNCPEVQKACDWLLSRQ 522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 653 EEDGGWGESHLSCPEQRYIPLEGnrSNLVQTAWAMMGLIHAGQAERDptPLHRAAKLIITSQLENGDFPQQEILGVFMN- 731
Cdd:TIGR01787 523 MPDGGWGEDCFSYEDPSYVGSGG--STPSQTGWALMALIAAGEADSE--AIERGVKYLLETQRPDGDWPQEYITGVGFPk 598
|
650 660
....*....|....*....|...
gi 30699377 732 TCMLHYATYRNIFPLWALAEYRK 754
Cdd:TIGR01787 599 NFYLKYTNYRNIFPLWALGRYRQ 621
|
|
| osq_cycl |
TIGR03463 |
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ... |
108-752 |
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: 539.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 108 ALQSSDGHWPAEITGTLFFLPPLVFCFYITGhleKIFDAEHRKEMLRHIYCHQNEDGGWGLHIEGKSVMFCTVLNYICLR 187
Cdd:TIGR03463 3 ALQDSAGDWEGDMGGCQFIIAIAVAGLHVMG---RPPDAEERAAIIAHFELHQLADGAWGLDPEAPGQVFFSVLAYVALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 188 MLGEGPNggrNNACKRARQWILDH-GGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLLPSFFPIHLGKTLCYTRMVYM 266
Cdd:TIGR03463 80 LLGLGKD---DAGLARARAWFHAQpEGPKASGAWGKFILALLGLYEREGLNAVPPELFLLPESLPFHPSRFWCHCRLIYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 267 PMSYLYGKRFVGPLT-PLIMLLRKELHLQPYEEINWNKARRLCAKEDMIYPHPLVQDLLWDTLHNFvepilTNWPLKKLv 345
Cdd:TIGR03463 157 GIAWLSGRGARAPESdPLLAAIRQEIFAEGYEQVDFGAARERVAPTDLFTPISFVLKAANDLLAGY-----ERLAGKAL- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 346 REKALRVAMEHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPDFMWVAED-GLKMQSFGS-QLWDTVF 423
Cdd:TIGR03463 231 RARALDFAFEQILAEDEATHYICIGPINGLLNCLAIFAHDPDGPDLAAHLEGLEAWFWEDDAeGLRMNGANSnALWDTAF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 424 AIQALLAC-DLSDETDDVLRKGHSFIKKSQVRENpSGDFKSMYRHISKGAWTLSDRDHGWQVSDCTAEALKCCMLLSMMP 502
Cdd:TIGR03463 311 AVQALAALgELDEEAKHALEEAAAFIDAAQMLAD-LADPQEAFRDPAKGGWCFSDGDHCWPISDCAAEALKALFALEELG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 503 AEVVGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFFTCVMAEREYVECTSAVIQALVLFKQLYPD 582
Cdd:TIGR03463 390 DNRISEALGAARLQDAVEFILSMQNADGGFATYELQRGGKLLELLNPSDMFGQCMTDLSYVECTAACLGALAAWLKHHPD 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 583 HRTKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKScLAVRKGVDFLLAIQEEDGGWGESH 662
Cdd:TIGR03463 470 LPDAKIDAAIRKAEEFIRRRQLDDGSFMGFWGICFTYATFFGAKGLIAAGAEPAD-MALQAAAAFLLEKQRADGAWGEHV 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 663 LSCPEQRYIplEGNRSNLVQTAWAMMGLIHAGQAERDPTplHRAAKLIITSQLENGDFPQQEILGVFMNTCMLHYATYRN 742
Cdd:TIGR03463 549 ESCLEARWV--EGKHGHAVMTAWALLALAAAGEAAHDAA--ERGIAWLCEQQGEDGGWPPEGIAGIFFGAAAIDYDAYLR 624
|
650
....*....|
gi 30699377 743 IFPLWALAEY 752
Cdd:TIGR03463 625 IFPTWALARC 634
|
|
| SqhC |
COG1657 |
Terpene cyclase SqhC [Lipid transport and metabolism]; |
97-756 |
3.80e-170 |
|
Terpene cyclase SqhC [Lipid transport and metabolism];
Pssm-ID: 441263 [Multi-domain] Cd Length: 644 Bit Score: 504.35 E-value: 3.80e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 97 DALRRAVSFYSALQSSDGHWPAEITGTlfFLPPlvfCFYITGH-LEKIFDAEHRKEMLRHIYCHQNEDGGWGLHIEGKSV 175
Cdd:COG1657 23 AAIAAAQALLLQQQDDGGWWGGELEAD--VTIA---AEYILLHhFLGPDDEELEAKIARYLRRQQNDDGGWPLYHGGPGD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 176 MFCTVLNYICLRMLGEGPNggrNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLLPSFFPIHLG 255
Cdd:COG1657 98 LSTTVKAYFALKLLGDDPD---APHMVRAREFILARGGAARANVFTKIWLALFGQYPWRGVPALPPEIMLLPRWFPFHIY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 256 KTLCYTRMVYMPMSYLYGKRFVGPLTPLImlLRKELHLQPYEEI-NWNKARRlcakedmiYPHPLVQDLLW-DTLHNFVE 333
Cdd:COG1657 175 KFSYWARTVIVPLLILYARKPVAPLPPGV--GIDELFVEPPEQVdYYFPAPR--------DRSPWSRFFLAlDRLLRAYE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 334 PiltnWPLKKLvREKALRVAMEHIHYEDENS-HYITIG-CVEKVLCMLACWIENPNGDHFKKHLARIPDFMWVAEDGLKM 411
Cdd:COG1657 245 R----LPPKPL-RRRALRKAEDWILERLEGDgGLGGIFpAMVNSLMALLALGYPPDHPVVRRALEALEKLLVETEDGARC 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 412 QSFGSQLWDTVFAIQALLACDLsDETDDVLRKGHSFIKKSQVREnpSGDFKSMYRHISKGAWTLSDRDHGWQVSDCTAEA 491
Cdd:COG1657 320 QPCVSPVWDTALAVQALQEAGL-PEDHPALERAADWLLSKQILV--KGDWAVKRPDVEPGGWAFQFANDHYPDVDDTAVV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 492 LKCCMLLSMMPAEVVGQKIDpeqlyDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFftCVMAEREYVECTSAVIQ 571
Cdd:COG1657 397 LMALLRLRLPDEPRYREAIE-----RAVEWILGMQSRDGGWGAFDKDNTKEWLNKIPFADH--GALLDPPTADVTARCLE 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 572 ALVLFKQlypdhrtKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTyKSCLAVRKGVDFLLAI 651
Cdd:COG1657 470 MLGQLGL-------TEDHPAIRRAVAYLRREQEPDGSWFGRWGVNYIYGTWSVLTGLNAAGVD-PDDPAIRRAVAWLLSI 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 652 QEEDGGWGESHLSCPEQRYIPLEgnRSNLVQTAWAMMGLIHAGQAERDptPLHRAAKLIITSQLENGDFPQQEILGV-FM 730
Cdd:COG1657 542 QNADGGWGEDCRSYEDPRYVGLG--PSTASQTAWALLALLAAGEADSP--AVARGIAYLLSTQREDGSWDEEYFTGTgFP 617
|
650 660
....*....|....*....|....*.
gi 30699377 731 NTCMLHYATYRNIFPLWALAEYRKAA 756
Cdd:COG1657 618 RVFYLRYHLYRQYFPLWALARYRNLR 643
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
399-752 |
2.07e-162 |
|
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: 473.24 E-value: 2.07e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 399 PDFMWVAEdglkmqsfGSQLWDTVFAIQALLACDLSDETDDVLRKGHSFIKKSQVRENPsGDFKSMYRHISKGAWTLSDR 478
Cdd:cd02889 14 PDGHWPGE--------YSQVWDTALALQALLEAGLAPEFDPALKKALEWLLKSQIRDNP-DDWKVKYRHLRKGGWAFSTA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 479 DHGWQVSDCTAEALKCCMLLSMMPAEvvGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELlnPTDFFTCVMA 558
Cdd:cd02889 85 NQGYPDSDDTAEALKALLRLQKKPPD--GKKVSRERLYDAVDWLLSMQNSNGGFAAFEPDNTYKYLEL--IPEVDGDIMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 559 EREYVECTSAVIQALVLFKQLYPDHRtKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTyKSC 638
Cdd:cd02889 161 DPPYVECTGSVLEALGLFGKLYPEHR-REIDPAIRRAVKYLEREQEPDGSWYGRWGVCFIYGTWFALEALAAAGED-ENS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 639 LAVRKGVDFLLAIQEEDGGWGESHLSCPEQRYipLEGNRSNLVQTAWAMMGLIHAGQAerDPTPLHRAAKLIITSQLENG 718
Cdd:cd02889 239 PYVRKACDWLLSKQNPDGGWGESYESYEDPSY--AGGGRSTVVQTAWALLALMAAGEP--DSEAVKRGVKYLLNTQQEDG 314
|
330 340 350
....*....|....*....|....*....|....
gi 30699377 719 DFPQQEILGVFMNTCMLHYATYRNIFPLWALAEY 752
Cdd:cd02889 315 DWPQEEITGVFFKNFYIRYHNYRNYFPLWALGRY 348
|
|
| hopene_cyclase |
TIGR01507 |
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ... |
92-758 |
3.37e-58 |
|
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: 209.36 E-value: 3.37e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 92 YKNATDALRRAVSFYSALQSSDGHWPAEITGTLFFLPPLVFCFYITGH-----LEKIfdaehrKEMLRHiycHQNEDGGW 166
Cdd:TIGR01507 11 TARTVEAIDRAVDYLLSCQKDEGYWWGELESNVTIEAEYVLLCHILDRvdrdrMEKI------RNYLLH---EQREDGTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 167 GLHIEGKSVMFCTVLNYICLRMLGEGPNggrNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLL 246
Cdd:TIGR01507 82 ALYPGGPGDLSTTVEAYVALKYIGMSRD---EPPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWRGVPMVPPEIMLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 247 PSFFPIHLGKTLCYTRMVYMPMSYLYGKRFVGPLTplimllrKELHLQPYEEINWNKARRLCAKEDMiyphPLVQDLLWD 326
Cdd:TIGR01507 159 PKRFPFNIYEFSSWARATVVPLSIVCSRKPVFPLP-------ERARVPELYETDVPKPRRRGAKGGT----GWGIFDALD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 327 TLHNFVEPILTnwplkKLVREKALRVAMEHIHYEDENS------------HYITIgcveKVLCMlacwieNPNGDHFKKH 394
Cdd:TIGR01507 228 RALHGYEKLSV-----HPFRRAAEIRALDWLLERQAGDgswggiqpamfnALIAL----KILGM------TQHDAFIKLG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 395 LARIPDFMWVAEDGLKMQSFGSQLWDTVFAIQALLACDLSDEtDDVLRKGHSFIKKSQVreNPSGDFKSMYRHISKGAWT 474
Cdd:TIGR01507 293 WEGIDLYGVELDDSWMFQACVSPVWDTALAVLALREAGLPAD-HDALVKAGEWLLDKQI--TVPGDWAVKRPNLEPGGWA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 475 LS-DRDHGWQVSDctaealKCCMLLSMMPAEVVGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFf 553
Cdd:TIGR01507 370 FQfDNVYYPDVDD------TAVVVWALNGLRLPDERRRRDAMTKAFRWIAGMQSSNGGWGAFDVDNTSDLLNHIPFCDF- 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 554 tcvmaeREYVECTSAVIQALVLfkQLYPDHRTKEIIKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGK 633
Cdd:TIGR01507 443 ------GAVTDPPTADVTARVL--ECLGSFGYDDAWPVIERAVEYLKREQEPDGSWFGRWGVNYLYGTGAVLSALKAVGI 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 634 TYKSClAVRKGVDFLLAIQEEDGGWGESHLSCPEQRYIPlEGNrSNLVQTAWAMMGLIHAGQAERdpTPLHRAAKLIITS 713
Cdd:TIGR01507 515 DTREP-YIQKALAWLESHQNPDGGWGEDCRSYEDPAYAG-KGA-STASQTAWALIALIAAGRAES--EAARRGVQYLVET 589
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 30699377 714 QLENGDFPQQEILGV-FMNTCMLHYATYRNIFPLWALAEYRKAAFA 758
Cdd:TIGR01507 590 QRPDGGWDEPYYTGTgFPGDFYLGYHMYRHVFPLLALARYKQAIER 635
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
393-752 |
4.28e-54 |
|
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: 188.91 E-value: 4.28e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 393 KHLARIPDfmwvAEDGLKMQSFGSQLWDTVFAIQALLACDLS----DETDDVLRKGHSFIKKSQvrenpsgdfksmyrhI 468
Cdd:cd00688 6 KYLLRYPY----GDGHWYQSLCGEQTWSTAWPLLALLLLLAAtgirDKADENIEKGIQRLLSYQ---------------L 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 469 SKGAWTLSDRdHGWQVSDCTAEALKCCMLLSMMPAevvgqkIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEwlelln 548
Cdd:cd00688 67 SDGGFSGWGG-NDYPSLWLTAYALKALLLAGDYIA------VDRIDLARALNWLLSLQNEDGGFREDGPGNHRI------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 549 ptdfftcvMAEREYVECTSAVIQALVLFKQLYPDhrtkeiiKSIEKGVQFIESKQTPDGSWhGNWGICFIYATWFALSGL 628
Cdd:cd00688 134 --------GGDESDVRLTAYALIALALLGKLDPD-------PLIEKALDYLLSCQNYDGGF-GPGGESHGYGTACAAAAL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 629 AAAGKTykSCLAVRKGVDFLLAIQEEDGGWGESHLscpeqryipLEGNRSNLVQTAWAMMGLIHAGQAeRDPTPLHRAAK 708
Cdd:cd00688 198 ALLGDL--DSPDAKKALRWLLSRQRPDGGWGEGRD---------RTNKLSDSCYTEWAAYALLALGKL-GDLEDAEKLVK 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 30699377 709 LIITSQLENGDFPQQEILgvfmntcmlHYATYRNIFPLWALAEY 752
Cdd:cd00688 266 WLLSQQNEDGGFSSKPGK---------SYDTQHTVFALLALSLY 300
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
416-754 |
3.28e-42 |
|
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: 156.34 E-value: 3.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 416 SQLWDTVFAIQALLACDLSDEtDDVLRKGHSFIKKSQVREnpSGDFKSMYRHISKGAWTLS-DRDHGWQVSDCTAealkc 494
Cdd:pfam13243 2 SPVWDTALALHALLEAGVPAD-HPALVKAAQWLLDRQVLV--KGDWAVKRPDLEPGGWAFQfANDHYPDVDDTAV----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 495 cMLLSMMPAEVVGQKIDPEQLYDSVNLLLSLQGEKGGLTAWEPVRAQEWLELLNPTDFFTcvMAEREYVECTSAVIQALV 574
Cdd:pfam13243 74 -VVLALDRVRLPDERRRDDAIARGIEWILGMQSKNGGWGAFDKDNTKYYLNKIPFADHGA--LLDPPTADVTARVLEMLG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 575 LFKqlYPDHRtkeiiKSIEKGVQFIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKSClAVRKGVDFLLAIQEE 654
Cdd:pfam13243 151 QLG--YPDDH-----PVAARALEYLKKEQEPDGSWFGRWGVNYIYGTWSVLCGLAAVGEDHNRP-YIRKAVDWLKSRQNP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 655 DGGWGESHLSCPEQRYipLEGNRSNLVQTAWAMMGLIHAGQAERDPTplHRAAKLIITSQLENGDFPQQEILGV-FMNTC 733
Cdd:pfam13243 223 DGGWGEDCESYKDPKL--AGRGPSTASQTAWALLALMAAGEVDSPAV--RRGIQYLLETQKPDGTWDEPYFTGTgFPRVF 298
|
330 340
....*....|....*....|.
gi 30699377 734 MLHYATYRNIFPLWALAEYRK 754
Cdd:pfam13243 299 YLKYHGYRNYFPLWALARYRN 319
|
|
| SQHop_cyclase_N |
pfam13249 |
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
99-357 |
8.11e-42 |
|
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: 154.18 E-value: 8.11e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 99 LRRAVSFYSALQSSDGHWPAE----ITGT------LFFLPPLvfcfyitghlekifDAEHRKEMLRHIYCHQNEDGGWGL 168
Cdd:pfam13249 1 IARAQDALLSLQHPDGHWVGEleanVTITaeyillRHFLGPD--------------DPELEAKIARYLRSQQREDGGWPL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 169 HIEGKSVMFCTVLNYICLRMLGEGPNggrNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSGTNPMPPEIWLLPS 248
Cdd:pfam13249 67 FHGGPGDLSTTVEAYFALKLLGDSPD---APHMVRAREFILARGGAAKANVFTRIWLALFGQYPWRGVPSMPPEIMLLPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 249 FFPIHLGKTLCYTRMVYMPMSYLYGKRFVGPLTPLIMLlrKELHLQPYEEInwnkaRRLCAKEDMIYPHPLVQDLlwDTL 328
Cdd:pfam13249 144 WFPFNIYKFSSWARTTIVPLLILSALKPVAPLPPGIGL--DELFVEPPENV-----RYYPRPHRLFSWTNLFLGL--DRV 214
|
250 260
....*....|....*....|....*....
gi 30699377 329 HNFVEPiltnWPLKKLvREKALRVAMEHI 357
Cdd:pfam13249 215 LKLYER----LPPKPL-RRRALRKAEEWI 238
|
|
| squa_tetra_cyc |
TIGR04277 |
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, ... |
160-754 |
4.91e-14 |
|
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: 75.82 E-value: 4.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 160 QNEDGGWgLHIEGKSV----MFCTVLNYICLRMLGEGPNggRNNACKRARQWILDHGGVTYIPSWGKIWLSILGIYDWSg 235
Cdd:TIGR04277 81 QFEDGSW-EQVEDANIetgqLDATIFNYWYLKAIGIDIH--IDAALKKAQEWIKANGGIEAAQTMTKFKLAAFGQYPWE- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 236 tnpmppEIWLLPSFfpihlgktLCYTRMVYmpmSYLYGK----RFVGPLTPLIMLLRkelhlqpYEEINWNKArrlcake 311
Cdd:TIGR04277 157 ------DLFKIPLF--------IFKKKGIF---KPLYIKditaQWVYPHLTALAYLQ-------NQRIIFNVA------- 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 312 dmiyphplVQDL--LWDtlhNFVEPILTNWPLKK--LVREKALRVAMEHIHYEDENSHYITIGCVEKVLCMLAcwIENPN 387
Cdd:TIGR04277 206 --------VADIreLWI---NKAKKGIKHQKKERpsFFIDNDLLILMDEIFKLKQPLGSFGAYTISTLLSLLA--FKDFQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 388 GDHFKKHLARIPDFMwvaEDGLKMQSF----------GS----QLWDTVFAIQALLAcdlSDETDDVLRKghsfIKKSQV 453
Cdd:TIGR04277 273 GKHPHKHKNEIQDAL---EDGLDFVEFnyfnfreayhGSlddgRWWDTILISWAMLE---SGEDKEKIFP----IVENML 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 454 RE--NPSGDFKSMYrhiskgawtlsdrDHGWqvsdcTAEALKCCMLLSMMP--AEVVGQKIDpeqlyDSVNLLLSLQGEK 529
Cdd:TIGR04277 343 KEglQPKGGIEYGY-------------DFEY-----APDADDTGLLLQVLSyyGEAFADAID-----EGAEFLFSMQNDD 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 530 GGLTAWEPVRAQEwlellNPTDFFTCVMAereyvectsAVIQALVLFKQLYPD---HRTKEIIKS--------IEKGVQF 598
Cdd:TIGR04277 400 GGFPAFDKGKMED-----NLLFKFAFKIA---------GIADSAEIFDPSCPDitaHILEGLGEFgdqanhdqIQKMIKY 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 599 IESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKSCLaVRKGVDFLLAIQEEDGGWGESHLSCPEqryiPLEGN-- 676
Cdd:TIGR04277 466 FMDTQEKFGSWEARWGINYIMAAGAVLPALAKMNYDLNEGW-AKNAINWLLNKQNADGGFGECTLSYND----PEKWNgi 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 677 -RSNLVQTAWAMMGLIHA-GQAERDPTPLHRAAK-LIITSQLENGDFPQQEILGVFMNTCM-LHYATYRNIFPLWALAEY 752
Cdd:TIGR04277 541 gKSTVTQTSWGLLALLAVeDHNDQIKEAADKAAQyLLDQFKRDDGEFKDHSTIGTGHRGLLyLQYPSYAQSFPLIALGRF 620
|
..
gi 30699377 753 RK 754
Cdd:TIGR04277 621 LD 622
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
592-632 |
1.29e-08 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 51.36 E-value: 1.29e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 30699377 592 IEKGVQFIESKQTPDGSWHGNWGIC-FIYATWFALSGLAAAG 632
Cdd:pfam00432 3 KEKLVDYLLSCQNEDGGFGGRPGGEsDTYYTYCALAALALLG 44
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
598-720 |
4.04e-06 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 48.93 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 598 FIESKQTPDGSWHGNWGICFIYATWFALSGLAAAGKTYKsclaVR-KGVDFLLAIQEEDGGWGeshlSCPEQRYIplegn 676
Cdd:COG5029 27 YLRASQNPDGGFAGRSGPSDLYSTYYAVRTLALLGESPK----WRdRVADLLSSLRVEDGGFA----KAPEGGAG----- 93
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 30699377 677 rsNLVQTAWAMMGLIHAGQAERDPTplhRAAKLIITSQLENGDF 720
Cdd:COG5029 94 --STYHTYLATLLAELLGRPPPDPD---RLVRFLISQQNDDGGF 132
|
|
| A2M_like |
cd02891 |
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
569-701 |
5.50e-05 |
|
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: 45.84 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 569 VIQALVLFKQLYPDHRTKeIIKSIEKGVQFIESKQTPDGS---WHGNWGicfiYATW---FALSGLAAAGK-TYKSCLAV 641
Cdd:cd02891 29 VLKYLDATGQLTPEIREK-ALEYIRKGYQRLLTYQRSDGSfsaWGNSDS----GSTWltaYVVKFLSQARKyIDVDENVL 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 642 RKGVDFLLAIQEEDGGWGESHlscPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDPT 701
Cdd:cd02891 104 ARALGWLVPQQKEDGSFRELG---PVIHREMKGGVDDSVSLTAYVLIALAEAGKACDASI 160
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
147-190 |
1.21e-04 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 40.19 E-value: 1.21e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 30699377 147 EHRKEMLRHIYCHQNEDGGWGLHIEGKSVMFCTVLNYICLRMLG 190
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
641-719 |
2.80e-04 |
|
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: 43.75 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 641 VRKGVDFLLAIQEEDGGWGeshlscpeqryipleGNRSNLVQTAWAMMGLIHAGQAERDPTPLHRAAKLIITSQ-LENGD 719
Cdd:cd02889 1 IRRALDFLLSLQAPDGHWP---------------GEYSQVWDTALALQALLEAGLAPEFDPALKKALEWLLKSQiRDNPD 65
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
496-720 |
7.67e-04 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 42.00 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 496 MLLSMMPAEVVG-QKIDPEQLYDSVNLLLSLQGEKGGLtAWEPVraqewlellnPTDFFTcvmaereyvecTSAVIQALV 574
Cdd:COG5029 1 MSLGVLSRLEGGsSKSTADFTDSHLDYLRASQNPDGGF-AGRSG----------PSDLYS-----------TYYAVRTLA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 575 LFKQLYPDHrtkeiiksiEKGVQFIESKQTPDGSW----HGNWGicFIYATWFALSGLAAAGKtykSCLAVRKGVDFLLA 650
Cdd:COG5029 59 LLGESPKWR---------DRVADLLSSLRVEDGGFakapEGGAG--STYHTYLATLLAELLGR---PPPDPDRLVRFLIS 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 651 IQEEDGGWGEShlscpeqryiplEGNRSNLVQTAWAMMGLIHAGQAerDPTPLHRAAKLIITSQLENGDF 720
Cdd:COG5029 125 QQNDDGGFEIS------------PGRRSDTNPTAAAIGALRALGAL--DDPIETKVIRFLRDVQSPEGGF 180
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
99-209 |
1.33e-03 |
|
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: 41.82 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 99 LRRAVSFYSALQSSDGHWPAEitgtlfFLPPLVFCFYITGHLEKIFDAEHRKEMLR-----------------HIYCHQN 161
Cdd:cd02889 1 IRRALDFLLSLQAPDGHWPGE------YSQVWDTALALQALLEAGLAPEFDPALKKalewllksqirdnpddwKVKYRHL 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 30699377 162 EDGGWGLHIEGKS--VMFCTVLNYICLRMLGEGPNGGRNN---ACKRARQWIL 209
Cdd:cd02889 75 RKGGWAFSTANQGypDSDDTAEALKALLRLQKKPPDGKKVsreRLYDAVDWLL 127
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
641-689 |
2.29e-03 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 36.34 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 30699377 641 VRKGVDFLLAIQEEDGGWGESHLSCPEQRYiplegnrSNLVQTAWAMMG 689
Cdd:pfam00432 3 KEKLVDYLLSCQNEDGGFGGRPGGESDTYY-------TYCALAALALLG 44
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
99-211 |
3.13e-03 |
|
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: 40.23 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 99 LRRAVSFYSALQSSDGHWPAEITG---TLFFLPPLVFCFYITGHLEKIFDAEHRKEMLRHIYCHQNEDGGWGLHIEGK-S 174
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCGeqtWSTAWPLLALLLLLAATGIRDKADENIEKGIQRLLSYQLSDGGFSGWGGNDyP 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 30699377 175 VMFCTVLNYICLRMLGEGPNGGRNNACkRARQWILDH 211
Cdd:cd00688 81 SLWLTAYALKALLLAGDYIAVDRIDLA-RALNWLLSL 116
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
445-720 |
3.51e-03 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 40.09 E-value: 3.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 445 HSFIKKsqvRENPSGDFksmyrhiskgAWTLSDRDHgwqVSDcTAEALKCCMLLSMMPAevvgqkiDPEQLydsVNLLLS 524
Cdd:COG1689 12 IEYVLK---RQNEDGGF----------CAYPGLPST---LAD-TYYAVRILKLLGEEVP-------NRDKT---IEFLES 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 525 LQGEKGGL----TAWEPVRAQEWLELLNPT-----DFFTCVMAEREYVECTSAVIQALV--LFKQLYPDhrtkeiIKSIE 593
Cdd:COG1689 65 CQDEEGGGfalyTTSYGLMALALLGIDPPDeqealEYLSDALPTKFAGGASDLEETYLAvaLLEALGAS------EPERE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 594 KGVQFIESKQTPDGSW---HGNwgicfIYATWFALSGLAAAG-KTYKSclavRKGVDFLLAIQEEDGGWGEShlscpeqr 669
Cdd:COG1689 139 KIREFLLSLRRPDGGFggkKPN-----LEDTYWALAALRRLGrDLPPA----DRVIAFILACQNEDGGFSKT-------- 201
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 30699377 670 yiplEGNRSNLVQTAWAMMGLIHAGQAERDPtplhRAAKLIITS-QLENGDF 720
Cdd:COG1689 202 ----PGSYSDLEATYYALRALKLLGEPPKNV----DKLLEFIAScQNSDGGF 245
|
|
| GGTase-II |
cd02894 |
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ... |
570-662 |
4.35e-03 |
|
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: 39.94 E-value: 4.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 570 IQALVLFKQLYpdhrtkEIIKSIEKGVQFIESKQTPDGSWHGN-WG---ICFIYAtwfALSGLAAAGKTYKSClaVRKGV 645
Cdd:cd02894 86 IQILALYDLLN------KIDENKEKIAKFIKGLQNEDGSFSGDkWGevdTRFSYC---AVLCLTLLGKLDLID--VDKAV 154
|
90 100
....*....|....*....|..
gi 30699377 646 DFLLAIQEEDGGWG-----ESH 662
Cdd:cd02894 155 DYLLSCYNFDGGFGcrpgaESH 176
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
91-211 |
6.06e-03 |
|
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: 39.46 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30699377 91 TYKNATDALRRAVSFYSALQSSDGHWPAEITG-------TLFFLppLVFCfyITGHLEKIfDAEHRKEMLRHIYCHQNED 163
Cdd:cd00688 46 IRDKADENIEKGIQRLLSYQLSDGGFSGWGGNdypslwlTAYAL--KALL--LAGDYIAV-DRIDLARALNWLLSLQNED 120
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 30699377 164 GGWGLHIEGKSVMFC----TVLNYICLRMLGEGPNGGRNNACKRARQWILDH 211
Cdd:cd00688 121 GGFREDGPGNHRIGGdesdVRLTAYALIALALLGKLDPDPLIEKALDYLLSC 172
|
|
| |
