|
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: 1186.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 1 MWRLKVADG-GNDPYIYSMNNFVGRQIWEFDPNAGTPEERAEVERIQNEFTANRFKGFPSADLLWRLQLLREKNFKQSIP 79
Cdd:PLN03012 1 MWKLKIAEGnGDDPYLFSTNNFAGRQTWEFDPDAGSPEELAAVEEARRIFYDDRFHVKASSDLIWRMQFLKEKKFEQRIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 80 AVKIEEGEEVSYEKAWDAMRRGAHFLAAIQASDGHWPSETSGPLFYNCPLLICMYIMGFLDAAFPPEHKKEMKRYIYNHQ 159
Cdd:PLN03012 81 PAKVEDAEKITFEIATNALRKGIHFFSALQASDGHWPAENAGPLFFLPPLVFCLYITGHLDEIFTQDHRKEILRYIYCHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 160 NEDGGWGLHVGGHSNMFCTTFNYISLRLLGEGPDVEP---VARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMP 236
Cdd:PLN03012 161 KEDGGWGLHIEGHSTMFCTTLNYICMRILGEGPDGGHdnaCGRARDWILDHGGATYIPSWGKTWLSILGVFDWSGSNPMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 237 PEYWMFPTWVPIHPSNMMCYTRITYMPMSYLYGKRFQAPLTPLVLQLREELHTEPYDKINWKKVRHMCATEDLYFPHPFV 316
Cdd:PLN03012 241 PEFWILPSFFPIHPAKMWCYCRLVYLPMSYLYGKRFVGPISPLILQLREEIYLQPYAEINWMKARHLCAKEDAYCPHPLI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 317 QDLLWDTLYLLSEPLMTRWPFNKLIRQKALDDTMRHIHYEDENSRYITIGCVEKPLCMLACWVEDPNSDYVKKHFARIPD 396
Cdd:PLN03012 321 QDLIWDCLYIFAEPFLACWPFNKLLREKALGLAMKHIHYEDENSRYITIGCVEKALCMLACWVEDPNGDHFKKHLLRISD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 397 YLWMAEDGMKMQSFGSQSWDAALAMQALLACNIPQEIDSALNTGHGFIKNSQVRNNPPGDYKSMFRYMSKGAWTFSDCDH 476
Cdd:PLN03012 401 YLWIAEDGMKMQSFGSQLWDSGFALQALLASNLSNEIPDVLRRGHDFIKNSQVGENPSGDFKNMYRHISKGAWTFSDRDH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 477 GWQVSDCTAENLKCCLLLSLLPPEMVGEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYWMEWLNPVEFLEDLIIEH 556
Cdd:PLN03012 481 GWQASDCTAEGFKCCLLFSMIAPDIVGPKMDPEQLHDAVNILLSLQSKNGGMTAWEPAGAPEWLELLNPTEMFADIVIEH 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 557 QHVECTSSALQAILLFRKQYPGHRRKEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENCEA 636
Cdd:PLN03012 561 EYNECTSSAIQALILFKQLYPDHRTEEINAFIKKAAEYIENIQMLDGSWYGNWGICFTYGTWFALAGLAAAGKTFNDCEA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 637 LRKGANFLIKIQNPEGGFGESYLSCPYKRYIPLDGKRSNLVQTAWGLMGLISSGQASVDPTPIHKAAKFLINSQLEDGDF 716
Cdd:PLN03012 641 IRKGVHFLLAAQKDNGGWGESYLSCPKKIYIAQEGEISNLVQTAWALMGLIHAGQAERDPIPLHRAAKLIINSQLENGDF 720
|
730 740 750
....*....|....*....|....*....|....*....
gi 2316531944 717 PQEEITGEFFKNCTLHFAAFREVFPVMALGEYCNKVPLP 755
Cdd:PLN03012 721 PQQEATGAFLKNCLLHYAAYRNIFPLWALAEYRARVPLP 759
|
|
| PLN02993 |
PLN02993 |
lupeol synthase |
1-748 |
0e+00 |
|
lupeol synthase
Pssm-ID: 215537 [Multi-domain] Cd Length: 763 Bit Score: 1131.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 1 MWRLKVADG-GNDPYIYSMNNFVGRQIWEFDPNAGTPEERAEVERIQNEFTANRFKGFPSADLLWRLQLLREKNFKQSIP 79
Cdd:PLN02993 1 MWKLKIGEGnGEDPYLFSSNNFVGRQTWEFDPKAGTPEERAAVEEARRSFLDNRSRVKGCSDLLWRMQFLKEAKFEQVIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 80 AVKIEEGEEVSYEKAWDAMRRGAHFLAAIQASDGHWPSETSGPLFYNCPLLICMYIMGFLDAAFPPEHKKEMKRYIYNHQ 159
Cdd:PLN02993 81 PVKIDRGEEITYETATNALRRGVSFFSALQASDGHWPGEITGPLFFLPPLVFCLYITGHLEEVFDAEHRKEMLRHIYCHQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 160 NEDGGWGLHVGGHSNMFCTTFNYISLRLLGEGPDV---EPVARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMP 236
Cdd:PLN02993 161 NEDGGWGLHIESKSVMFCTVLNYICLRMLGEGPNGgreNACKRARQWILDHGGVTYIPSWGKFWLSILGIYDWSGTNPMP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 237 PEYWMFPTWVPIHPSNMMCYTRITYMPMSYLYGKRFQAPLTPLVLQLREELHTEPYDKINWKKVRHMCATEDLYFPHPFV 316
Cdd:PLN02993 241 PEIWLLPSFLPIHLGKTLCYTRMVYMPMSYLYGKRFVGPITPLIMLLREELHLQPYEEINWNKARRLCAKEDMYYPHPLV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 317 QDLLWDTLYLLSEPLMTRWPFNKLIRQKALDDTMRHIHYEDENSRYITIGCVEKPLCMLACWVEDPNSDYVKKHFARIPD 396
Cdd:PLN02993 321 QDLIWDTLHNFVEPFLTRWPLNKLVREKALQVAMKHIHYEDENSHYITIGCVEKVLCMLACWIENPNGDHFKKHLARIPD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 397 YLWMAEDGMKMQSFGSQSWDAALAMQALLACNIPQEIDSALNTGHGFIKNSQVRNNPPGDYKSMFRYMSKGAWTFSDCDH 476
Cdd:PLN02993 401 YMWVAEDGMKMQSFGSQLWDTGFAIQALLASDLSDETDDVLRRGHNYIKKSQVRENPSGDFKSMYRHISKGAWTLSDRDH 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 477 GWQVSDCTAENLKCCLLLSLLPPEMVGEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYWMEWLNPVEFLEDLIIEH 556
Cdd:PLN02993 481 GWQVSDCTAEALKCCMLLSMMPADVVGQKIDPEQLYDSVNLLLSLQSENGGVTAWEPVRAYKWLELLNPTDFFANTMVER 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 557 QHVECTSSALQAILLFRKQYPGHRRKEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENCEA 636
Cdd:PLN02993 561 EYVECTSAVIQALVLFKQLYPDHRTKEIIKSIEKAVQFIESKQTPDGSWYGNWGICFIYATWFALGGLAAAGKTYNDCLA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 637 LRKGANFLIKIQNPEGGFGESYLSCPYKRYIPLDGKRSNLVQTAWGLMGLISSGQASVDPTPIHKAAKFLINSQLEDGDF 716
Cdd:PLN02993 641 MRKGVHFLLTIQRDDGGWGESYLSCPEQRYIPLEGNRSNLVQTAWAMMGLIHAGQAERDLIPLHRAAKLIITSQLENGDF 720
|
730 740 750
....*....|....*....|....*....|..
gi 2316531944 717 PQEEITGEFFKNCTLHFAAFREVFPVMALGEY 748
Cdd:PLN02993 721 PQQEILGAFMNTCMLHYATYRNTFPLWALAEY 752
|
|
| SQCY_1 |
cd02892 |
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ... |
98-748 |
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: 901.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 98 MRRGAHFLAAIQASDGHWPSETSGPLFYNCPLLICMYIMGFLDaafPPEHKKEMKRYIYNHQNEDGGWGLHVGGHSNMFC 177
Cdd:cd02892 1 IRRALEFLLSLQAPDGHWPGELEGPLFITAEYILLLYILGIPI---DPEHRKEIARYLRNHQNPDGGWGLHHEGPSTMFG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 178 TTFNYISLRLLGEGPDVEPVARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMFPTWVPIHPSNMMCYT 257
Cdd:cd02892 78 TVLNYVALRLLGVSPDDPHMVKARNWILSHGGAARIPVWGKIWLALLGVYPWEGVPPLPPELWLLPSWLPFHPYKFWCWA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 258 RITYMPMSYLYGKRFQAPLTPLVLQLREELHTEPYDKINWKKVRHmcATEDLYFPHPFVQDLLWDTLYLLseplmtRWPF 337
Cdd:cd02892 158 RTVYVPMSYLYGKRPVAPITPLVLSLRDELYVEPYEKINWYKHRN--DLYDYRPPWQRLFDALDRLLHWY------EPLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 338 NKLIRQKALDDTMRHIHYEDENSRYITIGCVEKPLCMLACWVED-PNSDYVKKHFARIPDYLWMAEDGMKM-QSFGSQSW 415
Cdd:cd02892 230 PKPLRRKALRKAYEWILYRDENTGYLGIIPPPKANNMLALWVLGyPDSPAFKRHLERIDDFLWLGPEGMKMcQTNGSQVW 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 416 DAALAMQALLACNIPQEIDSALNTGHGFIKNSQVRNNpPGDYKSMFRYMSKGAWTFSDCDHGWQVSDCTAENLKCCLLLS 495
Cdd:cd02892 310 DTALAVQALLEAGLAPEFDPALKKALDWLLESQILDN-PGDWKVKYRHLRKGGWAFSTANQGYPDSDDTAEALKALLRLQ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 496 LLPPEmvGEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYWMEWLNPVEFLEDLIIEHQHVECTSSALQAILLFRKQ 575
Cdd:cd02892 389 ELPPF--GEKVSRERLYDAVDWLLGMQNSNGGFAAFEPDNTYHWLENLNPFEDFGDIMIDPPYVECTGSVLEALGLFGKL 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 576 YPGHRRkEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENCEALRKGANFLIKIQNPEGGFG 655
Cdd:cd02892 467 YPGHRR-EIDPAIRRAVKYLLREQEPDGSWYGRWGVCYIYGTWFALEALAAAGEDYENSPYIRKACDFLLSKQNPDGGWG 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 656 ESYLSCPYKRYipLDGKRSNLVQTAWGLMGLISSGQAsvDPTPIHKAAKFLINSQLEDGDFPQEEITGEFFKNCTLHFAA 735
Cdd:cd02892 546 ESYLSYEDKSY--AGGGRSTVVQTAWALLALMAAGEP--DSEAVERGIKYLLNTQLPDGDWPQEEITGVGFPNFYIRYHN 621
|
650
....*....|...
gi 2316531944 736 FREVFPVMALGEY 748
Cdd:cd02892 622 YRNYFPLWALGRY 634
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
97-748 |
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: 721.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 97 AMRRGAHFLAAIQASDGHWPSETSGPLFYNCPLLICMYIMgflDAAFPpEHKKEMKRYIYNHQNEDGGWGLHVGGHSNMF 176
Cdd:TIGR01787 1 TARRAVEFLLSLQAPDGYWWGELEGPLTLLAEYVLLCHIA---DTPLP-GYREKIVRYLRHHQNEDGGWGLHIGGKSTVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 177 CTTFNYISLRLLGEGPDVEPVARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMFPTWVPIHPSNMMCY 256
Cdd:TIGR01787 77 GTVLAYVALKILGMSPDDPAMVRARNFILKQGGAVASPVFTKFWLALLGVYPWEGVPPLPPEIMLLPKWLPIHPSKSWCR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 257 TRITYMPMSYLYGKRFQAPLTPlvlqlREELHTEPyDKInwKKVRHMCATEDLYFPHPFVQDLLWDTLYLLSEPLMTRWp 336
Cdd:TIGR01787 157 CRMVYLPMSYCYGERLSAPIDP-----REELYVED-DSI--RAQRNNVAKEDLYTPHSWLLRALYGLLNLFYHPFLRKA- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 337 fnklIRQKALDDTMRHIHYEDensryiTIGCVEKPLCMLACWVED-PNSDYVKKHFARIPDYLWMAEDGMKMQSFGSQSW 415
Cdd:TIGR01787 228 ----LRKRALQWLYEHIAADG------SIGPISKAMAMLALWFLDgPNSPAFQKHLQRIDDYLWLQLDGMKMQGTGSQVW 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 416 DAALAMQALLACNI--PQEIDSALNTGHGFIKNSQVRNNPPGDYKsMFRYMSK-GAWTFSDCDHGW-QVSDCTAEnlKCC 491
Cdd:TIGR01787 298 DTAFAIQALRESGDhrLPEFHPALVKAHEWLLLSQIPDNPPGDWK-VYRHNLKpGGWAFSFLNCGYpDVDDTAVV--ALK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 492 LLLSLLPPemvgEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYWMEWLNPVEFLEDLIIEHQHVECTSSALQAILL 571
Cdd:TIGR01787 375 AVLLLQED----EHVKRDRLRDAVNWILGMQSSNGGFAAYDPDNTGEWLELLNPSEVFGDIMIDPPYVDVTARVIQALGA 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 572 FrkqypGHRRKEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENCEALRKGANFLIKIQNPE 651
Cdd:TIGR01787 451 F-----GHRADEIRNVLERALEYLRREQRADGSWFGRWGVNYTYGTGFVLSALAAAGRTYRNCPEVQKACDWLLSRQMPD 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 652 GGFGESYLSCPYKRYIPLDGkrSNLVQTAWGLMGLISSGQAsvDPTPIHKAAKFLINSQLEDGDFPQEEITGEFF-KNCT 730
Cdd:TIGR01787 526 GGWGEDCFSYEDPSYVGSGG--STPSQTGWALMALIAAGEA--DSEAIERGVKYLLETQRPDGDWPQEYITGVGFpKNFY 601
|
650
....*....|....*...
gi 2316531944 731 LHFAAFREVFPVMALGEY 748
Cdd:TIGR01787 602 LKYTNYRNIFPLWALGRY 619
|
|
| osq_cycl |
TIGR03463 |
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ... |
105-748 |
9.64e-157 |
|
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: 469.47 E-value: 9.64e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 105 LAAIQASDGHWPSETSGPLFYNCPLLICMYIMGfldAAFPPEHKKEMKRYIYNHQNEDGGWGLHVGGHSNMFCTTFNYIS 184
Cdd:TIGR03463 1 LAALQDSAGDWEGDMGGCQFIIAIAVAGLHVMG---RPPDAEERAAIIAHFELHQLADGAWGLDPEAPGQVFFSVLAYVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 185 LRLLGEGPDVEPVARGRNWVH-EHGGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMFPTWVPIHPSNMMCYTRITYMP 263
Cdd:TIGR03463 78 LRLLGLGKDDAGLARARAWFHaQPEGPKASGAWGKFILALLGLYEREGLNAVPPELFLLPESLPFHPSRFWCHCRLIYLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 264 MSYLYGKRFQAPLT-PLVLQLREELHTEPYDKINWKKVRHMCATEDLYFPHPFVQDLLWDTLYLLSeplmtRWPFnKLIR 342
Cdd:TIGR03463 158 IAWLSGRGARAPESdPLLAAIRQEIFAEGYEQVDFGAARERVAPTDLFTPISFVLKAANDLLAGYE-----RLAG-KALR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 343 QKALDDTMRHIHYEDENSRYITIGCVEKPLCMLACWVEDPNSDYVKKHFARIPDYLWMAED-GMKMQSFGSQS-WDAALA 420
Cdd:TIGR03463 232 ARALDFAFEQILAEDEATHYICIGPINGLLNCLAIFAHDPDGPDLAAHLEGLEAWFWEDDAeGLRMNGANSNAlWDTAFA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 421 MQALLAC-NIPQEIDSALNTGHGFIKNSQVRNNPpGDYKSMFRYMSKGAWTFSDCDHGWQVSDCTAENLKCCLLLSLLPP 499
Cdd:TIGR03463 312 VQALAALgELDEEAKHALEEAAAFIDAAQMLADL-ADPQEAFRDPAKGGWCFSDGDHCWPISDCAAEALKALFALEELGD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 500 EMVGEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYWMEWLNPVEFLEDLIIEHQHVECTSSALQAILLFRKQYPGH 579
Cdd:TIGR03463 391 NRISEALGAARLQDAVEFILSMQNADGGFATYELQRGGKLLELLNPSDMFGQCMTDLSYVECTAACLGALAAWLKHHPDL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 580 RRKEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENcEALRKGANFLIKIQNPEGGFGESYL 659
Cdd:TIGR03463 471 PDAKIDAAIRKAEEFIRRRQLDDGSFMGFWGICFTYATFFGAKGLIAAGAEPAD-MALQAAAAFLLEKQRADGAWGEHVE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 660 SCPYKRYIplDGKRSNLVQTAWGLMGLISSGQASVDptPIHKAAKFLINSQLEDGDFPQEEITGEFFKNCTLHFAAFREV 739
Cdd:TIGR03463 550 SCLEARWV--EGKHGHAVMTAWALLALAAAGEAAHD--AAERGIAWLCEQQGEDGGWPPEGIAGIFFGAAAIDYDAYLRI 625
|
....*....
gi 2316531944 740 FPVMALGEY 748
Cdd:TIGR03463 626 FPTWALARC 634
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
409-748 |
2.10e-144 |
|
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: 427.02 E-value: 2.10e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 409 SFGSQSWDAALAMQALLACNIPQEIDSALNTGHGFIKNSQVRNNPPgDYKSMFRYMSKGAWTFSDCDHGWQVSDCTAENL 488
Cdd:cd02889 20 GEYSQVWDTALALQALLEAGLAPEFDPALKKALEWLLKSQIRDNPD-DWKVKYRHLRKGGWAFSTANQGYPDSDDTAEAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 489 KCCLLLSLLPPEmvGEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYWMEWlnPVEFLEDLIIEHQHVECTSSALQA 568
Cdd:cd02889 99 KALLRLQKKPPD--GKKVSRERLYDAVDWLLSMQNSNGGFAAFEPDNTYKYLEL--IPEVDGDIMIDPPYVECTGSVLEA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 569 ILLFRKQYPGHRRkEINNFINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTyENCEALRKGANFLIKIQ 648
Cdd:cd02889 175 LGLFGKLYPEHRR-EIDPAIRRAVKYLEREQEPDGSWYGRWGVCFIYGTWFALEALAAAGED-ENSPYVRKACDWLLSKQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 649 NPEGGFGESYLSCPYKRYipLDGKRSNLVQTAWGLMGLISSGQAsvDPTPIHKAAKFLINSQLEDGDFPQEEITGEFFKN 728
Cdd:cd02889 253 NPDGGWGESYESYEDPSY--AGGGRSTVVQTAWALLALMAAGEP--DSEAVKRGVKYLLNTQQEDGDWPQEEITGVFFKN 328
|
330 340
....*....|....*....|
gi 2316531944 729 CTLHFAAFREVFPVMALGEY 748
Cdd:cd02889 329 FYIRYHNYRNYFPLWALGRY 348
|
|
| SqhC |
COG1657 |
Terpene cyclase SqhC [Lipid transport and metabolism]; |
96-751 |
3.27e-144 |
|
Terpene cyclase SqhC [Lipid transport and metabolism];
Pssm-ID: 441263 [Multi-domain] Cd Length: 644 Bit Score: 437.33 E-value: 3.27e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 96 DAMRRGAHFLAAIQASDGHWPSETSGPLFYNCPLLICMYIMGfldaAFPPEHKKEMKRYIYNHQNEDGGWGLHVGGHSNM 175
Cdd:COG1657 23 AAIAAAQALLLQQQDDGGWWGGELEADVTIAAEYILLHHFLG----PDDEELEAKIARYLRRQQNDDGGWPLYHGGPGDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 176 FCTTFNYISLRLLGEGPDVEPVARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMFPTWVPIHPSNMMC 255
Cdd:COG1657 99 STTVKAYFALKLLGDDPDAPHMVRAREFILARGGAARANVFTKIWLALFGQYPWRGVPALPPEIMLLPRWFPFHIYKFSY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 256 YTRITYMPMSYLYGKRFQAPLTPLVlqLREELHTEPYDKInwkkvrhmcateDLYFPHPFvQDLLWDTLYLLSEPLMTRW 335
Cdd:COG1657 179 WARTVIVPLLILYARKPVAPLPPGV--GIDELFVEPPEQV------------DYYFPAPR-DRSPWSRFFLALDRLLRAY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 336 -PFN-KLIRQKALDDTMRHIHYEDENS-RYITIG-CVEKPLCMLACWVEDPNSDYVKKHFARIPDYLWMAEDGMKMQSFG 411
Cdd:COG1657 244 eRLPpKPLRRRALRKAEDWILERLEGDgGLGGIFpAMVNSLMALLALGYPPDHPVVRRALEALEKLLVETEDGARCQPCV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 412 SQSWDAALAMQALLACNIPQEiDSALNTGHGFIKNSQVRNnpPGDYKSMFRYMSKGAWTFSDCDHGWQVSDCTAENLKCC 491
Cdd:COG1657 324 SPVWDTALAVQALQEAGLPED-HPALERAADWLLSKQILV--KGDWAVKRPDVEPGGWAFQFANDHYPDVDDTAVVLMAL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 492 LLLSLLPPEMVGEKMEperfyDAVNVILNMQSKNGGLPAWEPASRYYWMEWLNPVEFleDLIIEHQHVECTSSALQAilL 571
Cdd:COG1657 401 LRLRLPDEPRYREAIE-----RAVEWILGMQSRDGGWGAFDKDNTKEWLNKIPFADH--GALLDPPTADVTARCLEM--L 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 572 FRKQYPGHRRKeinnfINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTyENCEALRKGANFLIKIQNPE 651
Cdd:COG1657 472 GQLGLTEDHPA-----IRRAVAYLRREQEPDGSWFGRWGVNYIYGTWSVLTGLNAAGVD-PDDPAIRRAVAWLLSIQNAD 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 652 GGFGESYLSCPYKRYIPLDgkRSNLVQTAWGLMGLISSGQAsvDPTPIHKAAKFLINSQLEDGDFPQEEITG-EFFKNCT 730
Cdd:COG1657 546 GGWGEDCRSYEDPRYVGLG--PSTASQTAWALLALLAAGEA--DSPAVARGIAYLLSTQREDGSWDEEYFTGtGFPRVFY 621
|
650 660
....*....|....*....|.
gi 2316531944 731 LHFAAFREVFPVMALGEYCNK 751
Cdd:COG1657 622 LRYHLYRQYFPLWALARYRNL 642
|
|
| hopene_cyclase |
TIGR01507 |
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ... |
90-750 |
2.62e-60 |
|
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: 215.14 E-value: 2.62e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 90 SYEKAWDAMRRGAHFLAAIQASDGHWpsetSGPLFYNCPL----LICMYIMGFLDAAfpPEHKkeMKRYIYNHQNEDGGW 165
Cdd:TIGR01507 10 ATARTVEAIDRAVDYLLSCQKDEGYW----WGELESNVTIeaeyVLLCHILDRVDRD--RMEK--IRNYLLHEQREDGTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 166 GLHVGGHSNMFCTTFNYISLRLLGEGPDVEPVARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMFPTW 245
Cdd:TIGR01507 82 ALYPGGPGDLSTTVEAYVALKYIGMSRDEPPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWRGVPMVPPEIMLLPKR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 246 VPIHPSNMMCYTRITYMPMSYLYGKRFQAPLtPLVLQLREELHTEPydkinwKKVRHmcatedlYFPH---PFVQDLLWD 322
Cdd:TIGR01507 162 FPFNIYEFSSWARATVVPLSIVCSRKPVFPL-PERARVPELYETDV------PKPRR-------RGAKggtGWGIFDALD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 323 TLYLLSEPLMTRwPFNKLIRQKALDDTMRHIHYEDEnsryitIGCVEKP----LCMLACWVEDPNSDYVKKHFARIPDYL 398
Cdd:TIGR01507 228 RALHGYEKLSVH-PFRRAAEIRALDWLLERQAGDGS------WGGIQPAmfnaLIALKILGMTQHDAFIKLGWEGIDLYG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 399 WMAEDGMKMQSFGSQSWDAALAMQALLACNIPQEiDSALNTGHGFIKNSQVrnNPPGDYKSMFRYMSKGAWTFS-DCDHG 477
Cdd:TIGR01507 301 VELDDSWMFQACVSPVWDTALAVLALREAGLPAD-HDALVKAGEWLLDKQI--TVPGDWAVKRPNLEPGGWAFQfDNVYY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 478 WQVSDCTAenLKCCLLLSLLPPEmvgekmepERFYDAVNVILN----MQSKNGGLPAWEPASRYYWmewLNPVEFLE-DL 552
Cdd:TIGR01507 378 PDVDDTAV--VVWALNGLRLPDE--------RRRRDAMTKAFRwiagMQSSNGGWGAFDVDNTSDL---LNHIPFCDfGA 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 553 IIEHQHVECTSSALQAILLFRKQYPGHRrkeinnfINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALsmAGKTYE 632
Cdd:TIGR01507 445 VTDPPTADVTARVLECLGSFGYDDAWPV-------IERAVEYLKREQEPDGSWFGRWGVNYLYGTGAVLSAL--KAVGID 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 633 NCE-ALRKGANFLIKIQNPEGGFGESYLSCPYKRYiplDGK-RSNLVQTAWGLMGLISSGQAsvDPTPIHKAAKFLINSQ 710
Cdd:TIGR01507 516 TREpYIQKALAWLESHQNPDGGWGEDCRSYEDPAY---AGKgASTASQTAWALIALIAAGRA--ESEAARRGVQYLVETQ 590
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2316531944 711 LEDGDFPQEEITGEFF-KNCTLHFAAFREVFPVMALGEYCN 750
Cdd:TIGR01507 591 RPDGGWDEPYYTGTGFpGDFYLGYHMYRHVFPLLALARYKQ 631
|
|
| SQHop_cyclase_N |
pfam13249 |
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
98-302 |
2.21e-40 |
|
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: 150.33 E-value: 2.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 98 MRRGAHFLAAIQASDGHWpsetSGPLFYNCPL----LICMYIMGFLDAAfpPEHKkeMKRYIYNHQNEDGGWGLHVGGHS 173
Cdd:pfam13249 1 IARAQDALLSLQHPDGHW----VGELEANVTItaeyILLRHFLGPDDPE--LEAK--IARYLRSQQREDGGWPLFHGGPG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 174 NMFCTTFNYISLRLLGEGPDVEPVARGRNWVHEHGGVTSILSWGKTWLSILNVFDWSASNPMPPEYWMFPTWVPIHPSNM 253
Cdd:pfam13249 73 DLSTTVEAYFALKLLGDSPDAPHMVRAREFILARGGAAKANVFTRIWLALFGQYPWRGVPSMPPEIMLLPRWFPFNIYKF 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2316531944 254 MCYTRITYMPMSYLYGKRFQAPLTPLVlqLREELHTEPYDKINWKKVRH 302
Cdd:pfam13249 153 SSWARTTIVPLLILSALKPVAPLPPGI--GLDELFVEPPENVRYYPRPH 199
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
389-748 |
1.03e-36 |
|
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: 139.99 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 389 KHFARIPDYLwmaeDGMKMQSFGSQSWDA----ALAMQALLACNIPQEIDSALNTGHGFIKNSQVRNnppgdyksmfrym 464
Cdd:cd00688 6 KYLLRYPYGD----GHWYQSLCGEQTWSTawplLALLLLLAATGIRDKADENIEKGIQRLLSYQLSD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 465 skGAWTFSDcDHGWQVSDCTAENLKCCLLLSLLppemvgEKMEPERFYDAVNVILNMQSKNGGLPAWEPASRYYwmewln 544
Cdd:cd00688 69 --GGFSGWG-GNDYPSLWLTAYALKALLLAGDY------IAVDRIDLARALNWLLSLQNEDGGFREDGPGNHRI------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 545 pvefledlIIEHQHVECTSSALQAILLFRKQYPghrrkeiNNFINKAVQFLQDIQLPDGSWyGNWGICYTYGTWFALKAL 624
Cdd:cd00688 134 --------GGDESDVRLTAYALIALALLGKLDP-------DPLIEKALDYLLSCQNYDGGF-GPGGESHGYGTACAAAAL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 625 SMAGKTyeNCEALRKGANFLIKIQNPEGGFGESYLscpykryipLDGKRSNLVQTAWGLMGLISSGQASvDPTPIHKAAK 704
Cdd:cd00688 198 ALLGDL--DSPDAKKALRWLLSRQRPDGGWGEGRD---------RTNKLSDSCYTEWAAYALLALGKLG-DLEDAEKLVK 265
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2316531944 705 FLINSQLEDGDFPQEEItgefFKNCTLHFaafreVFPVMALGEY 748
Cdd:cd00688 266 WLLSQQNEDGGFSSKPG----KSYDTQHT-----VFALLALSLY 300
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
514-750 |
8.87e-36 |
|
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: 137.85 E-value: 8.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 514 AVNVILNMQSKNGGLPAWEPASRYYWmewLNPVEF--LEDLIiEHQHVECTSSALQ--AILLFRKQYPGHRRkeinnfin 589
Cdd:pfam13243 96 GIEWILGMQSKNGGWGAFDKDNTKYY---LNKIPFadHGALL-DPPTADVTARVLEmlGQLGYPDDHPVAAR-------- 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 590 kAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGkTYENCEALRKGANFLIKIQNPEGGFGESYLScpYKRYiPL 669
Cdd:pfam13243 164 -ALEYLKKEQEPDGSWFGRWGVNYIYGTWSVLCGLAAVG-EDHNRPYIRKAVDWLKSRQNPDGGWGEDCES--YKDP-KL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 670 DGK-RSNLVQTAWGLMGLISSGQasVDPTPIHKAAKFLINSQLEDGDFPQEEITGEFF-KNCTLHFAAFREVFPVMALGE 747
Cdd:pfam13243 239 AGRgPSTASQTAWALLALMAAGE--VDSPAVRRGIQYLLETQKPDGTWDEPYFTGTGFpRVFYLKYHGYRNYFPLWALAR 316
|
...
gi 2316531944 748 YCN 750
Cdd:pfam13243 317 YRN 319
|
|
| squa_tetra_cyc |
TIGR04277 |
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, ... |
588-748 |
7.68e-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: 75.05 E-value: 7.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 588 INKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENcEALRKGANFLIKIQNPEGGFGESYLScpYKRYI 667
Cdd:TIGR04277 459 IQKMIKYFMDTQEKFGSWEARWGINYIMAAGAVLPALAKMNYDLNE-GWAKNAINWLLNKQNADGGFGECTLS--YNDPE 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 668 PLDG-KRSNLVQTAWGLMGLIS-SGQASVDPTPIHKAAKFLINS-QLEDGDFPQEEITGEFFKNCT-LHFAAFREVFPVM 743
Cdd:TIGR04277 536 KWNGiGKSTVTQTSWGLLALLAvEDHNDQIKEAADKAAQYLLDQfKRDDGEFKDHSTIGTGHRGLLyLQYPSYAQSFPLI 615
|
....*
gi 2316531944 744 ALGEY 748
Cdd:TIGR04277 616 ALGRF 620
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
588-716 |
2.66e-09 |
|
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: 59.10 E-value: 2.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 588 INKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENC----EALRKGANFLIKIQNPEGGFGESYlscpy 663
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAATGIRdkadENIEKGIQRLLSYQLSDGGFSGWG----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2316531944 664 kryiplDGKRSNLVQTAWGLMGLISSGQA-SVDPTPIHKAAKFLINSQLEDGDF 716
Cdd:cd00688 76 ------GNDYPSLWLTAYALKALLLAGDYiAVDRIDLARALNWLLSLQNEDGGF 123
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
588-628 |
1.34e-08 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 51.36 E-value: 1.34e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2316531944 588 INKAVQFLQDIQLPDGSWYGNWGICY-TYGTWFALKALSMAG 628
Cdd:pfam00432 3 KEKLVDYLLSCQNEDGGFGGRPGGESdTYYTYCALAALALLG 44
|
|
| A2M_like |
cd02891 |
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
581-706 |
6.85e-08 |
|
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: 54.70 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 581 RKEINNFINKAVQFLQDIQLPDGSwYGNWGICYTYGTW---FALKALSMAGK-TYENCEALRKGANFLIKIQNPEGGFGE 656
Cdd:cd02891 44 REKALEYIRKGYQRLLTYQRSDGS-FSAWGNSDSGSTWltaYVVKFLSQARKyIDVDENVLARALGWLVPQQKEDGSFRE 122
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2316531944 657 SYlscPYKRYIPLDGKRSNLVQTAWGLMGLISSGQASvdPTPIHKAAKFL 706
Cdd:cd02891 123 LG---PVIHREMKGGVDDSVSLTAYVLIALAEAGKAC--DASIEKALAYL 167
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
146-189 |
8.46e-08 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 49.05 E-value: 8.46e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2316531944 146 EHKKEMKRYIYNHQNEDGGWGLHVGGHSNMFCTTFNYISLRLLG 189
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
587-716 |
1.65e-07 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 53.17 E-value: 1.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 587 FINKAVQFLQDIQLPDGSWYGNWGICYTYGTWFALKALSMAGKTYENCEALrkgANFLIKIQNPEGGFGESYlscpykry 666
Cdd:COG5029 20 FTDSHLDYLRASQNPDGGFAGRSGPSDLYSTYYAVRTLALLGESPKWRDRV---ADLLSSLRVEDGGFAKAP-------- 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2316531944 667 iplDGKRSNLVQTAWGLMGLISSGQASVDPTpihKAAKFLINSQLEDGDF 716
Cdd:COG5029 89 ---EGGAGSTYHTYLATLLAELLGRPPPDPD---RLVRFLISQQNDDGGF 132
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
558-716 |
2.05e-07 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 52.79 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 558 HVECTSSALQAILLFRKQYPgHRrkeinnfiNKAVQFLQDIQLPDG-------SWYGNwgicyTYGTWFALKALSMAGkt 630
Cdd:COG5029 46 DLYSTYYAVRTLALLGESPK-WR--------DRVADLLSSLRVEDGgfakapeGGAGS-----TYHTYLATLLAELLG-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 631 yENCEALRKGANFLIKIQNPEGGFGESYlscpykryipldGKRSNLVQTAWGLMGLISSGQAsvDPTPIHKAAKFLINSQ 710
Cdd:COG5029 110 -RPPPDPDRLVRFLISQQNDDGGFEISP------------GRRSDTNPTAAAIGALRALGAL--DDPIETKVIRFLRDVQ 174
|
....*.
gi 2316531944 711 LEDGDF 716
Cdd:COG5029 175 SPEGGF 180
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
80-262 |
1.27e-06 |
|
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: 51.01 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 80 AVKIEEGEEVSYEKAWDAMRRGAHFLAAIQASDGHWpsetSGPLFYNCPLLICMY--IMGFLDA----AFPPEHKKEMKR 153
Cdd:cd00688 36 ALLLLLAATGIRDKADENIEKGIQRLLSYQLSDGGF----SGWGGNDYPSLWLTAyaLKALLLAgdyiAVDRIDLARALN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 154 YIYNHQNEDGGWGLH-------VGGHSNMFCTTFNYISLRLLGEGPDVEPVARGRNWV--------------HEHGGVTS 212
Cdd:cd00688 112 WLLSLQNEDGGFREDgpgnhriGGDESDVRLTAYALIALALLGKLDPDPLIEKALDYLlscqnydggfgpggESHGYGTA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2316531944 213 ILSWGktwLSILN---------VFDWSASNPMPPEYWMFPTWVPIHPSNmMCYTRITYM 262
Cdd:cd00688 192 CAAAA---LALLGdldspdakkALRWLLSRQRPDGGWGEGRDRTNKLSD-SCYTEWAAY 246
|
|
| PTase |
cd02890 |
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ... |
558-657 |
4.45e-06 |
|
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They 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 the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes.
Pssm-ID: 239220 [Multi-domain] Cd Length: 286 Bit Score: 49.12 E-value: 4.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 558 HVECTSSALQAILLFRKqypghrrkEINNFINKA--VQFLQDIQLPDGSWYGN-WG-----ICYTygtwfALKALSMAGK 629
Cdd:cd02890 76 HLASTYAAVLSLAILGD--------DALSRIDREkiYKFLSSLQNPDGSFRGDlGGevdtrFVYC-----ALSILSLLNI 142
|
90 100
....*....|....*....|....*....
gi 2316531944 630 -TYENCEALrkgANFLIKIQNPEGGFGES 657
Cdd:cd02890 143 lTDIDKEKL---IDYILSCQNYDGGFGGV 168
|
|
| complement_C3_C4_C5 |
cd02896 |
Proteins similar to C3, C4 and C5 of vertebrate complement. The vertebrate complement system, ... |
579-658 |
9.61e-06 |
|
Proteins similar to C3, C4 and C5 of vertebrate complement. The vertebrate complement system, comprised of a large number of distinct plasma proteins, 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: 239226 [Multi-domain] Cd Length: 297 Bit Score: 48.04 E-value: 9.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 579 HRRKEINNFINKAVQFLQDIQLPDGSwYGNWGiCYTYGTW---FALKALSMAGKTYE-NCEALRKGANFLIKIQNPEGGF 654
Cdd:cd02896 45 ERRDEALKYIRQGYQRQLSYRKPDGS-YAAWK-NRPSSTWltaFVVKVFSLARKYIPvDQNVICGSVNWLISNQKPDGSF 122
|
....
gi 2316531944 655 GESY 658
Cdd:cd02896 123 QEPS 126
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
98-165 |
1.06e-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: 48.37 E-value: 1.06e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2316531944 98 MRRGAHFLAAIQASDGHWPSETSgplfyncPLLICMY-IMGFLDAAFPPEHKKEMKR---YIYNHQ-NEDGGW 165
Cdd:cd02889 1 IRRALDFLLSLQAPDGHWPGEYS-------QVWDTALaLQALLEAGLAPEFDPALKKaleWLLKSQiRDNPDD 66
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
100-207 |
2.08e-05 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 47.01 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 100 RGAHFLAAIQASDGHW---PSETSGPLFYNCPLLICMYIMGFldaafPPEHKKEMKRYIYNHQNEDGGWGLHVGGHSNMF 176
Cdd:COG5029 69 RVADLLSSLRVEDGGFakaPEGGAGSTYHTYLATLLAELLGR-----PPPDPDRLVRFLISQQNDDGGFEISPGRRSDTN 143
|
90 100 110
....*....|....*....|....*....|...
gi 2316531944 177 CTTFNYISLRLLGEG--PDVEPVARgrnWVHEH 207
Cdd:COG5029 144 PTAAAIGALRALGALddPIETKVIR---FLRDV 173
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
98-204 |
2.49e-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: 46.77 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 98 MRRGAHFLAAIQASDGHWPSETSGplfynCPLLICMY-IMGFLDAAFPPEHKKEMKRYI-------YNHQNEDGGWGLHV 169
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCG-----EQTWSTAWpLLALLLLLAATGIRDKADENIekgiqrlLSYQLSDGGFSGWG 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 2316531944 170 GGH-SNMFCTTFNYISLRLLGEGPDVEP--VARGRNWV 204
Cdd:cd00688 76 GNDyPSLWLTAYALKALLLAGDYIAVDRidLARALNWL 113
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
555-658 |
4.07e-05 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 45.87 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 555 EHQHVECTSSALQAILLFRKQYPGHRRkeinnfinkAVQFLQDIQLPDGSW----YGNWGICYTYgtwFALKALSMAGKT 630
Cdd:COG1689 157 KKPNLEDTYWALAALRRLGRDLPPADR---------VIAFILACQNEDGGFsktpGSYSDLEATY---YALRALKLLGEP 224
|
90 100
....*....|....*....|....*...
gi 2316531944 631 YENCEALRkgaNFLIKIQNPEGGFGESY 658
Cdd:COG1689 225 PKNVDKLL---EFIASCQNSDGGFRRSP 249
|
|
| osq_cycl |
TIGR03463 |
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ... |
97-209 |
4.52e-03 |
|
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: 40.36 E-value: 4.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 97 AMRRGAHFLAAIQASDGHWPsetsGPLFYNCPLLICMYIMGFLDAAFPPEHK--KEMKRYIYNHQNEDGGWGLHV----- 169
Cdd:TIGR03463 478 AIRKAEEFIRRRQLDDGSFM----GFWGICFTYATFFGAKGLIAAGAEPADMalQAAAAFLLEKQRADGAWGEHVescle 553
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2316531944 170 -----GGHSNMFCTTFNYISLRLLGEGPDvEPVARGRNWVHEHGG 209
Cdd:TIGR03463 554 arwveGKHGHAVMTAWALLALAAAGEAAH-DAAERGIAWLCEQQG 597
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
90-166 |
9.07e-03 |
|
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: 38.85 E-value: 9.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2316531944 90 SYEKAWDAMRRGAHFLAAIQASDGHWPSETSGPLFYNCpllicMYIMGFLDAAFPPEHKKEMKR---YIYNHQNEDGGWG 166
Cdd:pfam13243 153 GYPDDHPVAARALEYLKKEQEPDGSWFGRWGVNYIYGT-----WSVLCGLAAVGEDHNRPYIRKavdWLKSRQNPDGGWG 227
|
|
| |
