|
Name |
Accession |
Description |
Interval |
E-value |
| SqhC |
COG1657 |
Terpene cyclase SqhC [Lipid transport and metabolism]; |
30-658 |
0e+00 |
|
Terpene cyclase SqhC [Lipid transport and metabolism];
Pssm-ID: 441263 [Multi-domain] Cd Length: 644 Bit Score: 714.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 30 REVQQEINRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLGIHDEHLMEKLTAHITSLQHDNGAWKLYPDEHeGN 109
Cdd:COG1657 19 SLLDAAIAAAQALLLQQQDDGGWWGGELEADVTIAAEYILLHHFLGPDDEELEAKIARYLRRQQNDDGGWPLYHGGP-GD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 110 LSTTIDSYYALLLSGkYTKDEPRMALARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIALFLPSFPVSFYDF 189
Cdd:COG1657 98 LSTTVKAYFALKLLG-DDPDAPHMVRAREFILARGGAARANVFTKIWLALFGQYPWRGVPALPPEIMLLPRWFPFHIYKF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 190 VGYARVHLAPMMIVADRKYAKKPDNAPDLSDLYADTPISRGLYPHRFLENFLKEGqsFLASIHDSLQRL-PFLPGQLHKL 268
Cdd:COG1657 177 SYWARTVIVPLLILYARKPVAPLPPGVGIDELFVEPPEQVDYYFPAPRDRSPWSR--FFLALDRLLRAYeRLPPKPLRRR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 269 ALRRLEQYILARIEPDGTLYNYSTSTFFMIFALLARGFSPKDPLIQKAMQGLSDSVYVYENGAHLQLATSAVWDTALLTS 348
Cdd:COG1657 255 ALRKAEDWILERLEGDGGLGGIFPAMVNSLMALLALGYPPDHPVVRRALEALEKLLVETEDGARCQPCVSPVWDTALAVQ 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 349 SLQKSGLSTTHPAIQKANRYLLQKQQHTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTAALRSLRLLSRTDITT-AAA 427
Cdd:COG1657 335 ALQEAGLPEDHPALERAADWLLSKQILVKGDWAVKRPDVEPGGWAFQFANDHYPDVDDTAVVLMALLRLRLPDEPRyREA 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 428 WKRGLEWLLSMQNDDGGWPAFERNTDADFIRQLPIEGADTVsTDPSSADLTGRTLEFLGNYaGRTLTDPHVEKGVRWLLN 507
Cdd:COG1657 415 IERAVEWILGMQSRDGGWGAFDKDNTKEWLNKIPFADHGAL-LDPPTADVTARCLEMLGQL-GLTEDHPAIRRAVAYLRR 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 508 HQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVANQNPDGGWGESCQSDQKKTYVPLGASTPSQTA 587
Cdd:COG1657 493 EQEPDGSWFGRWGVNYIYGTWSVLTGLNAAGVDPDDPAIRRAVAWLLSIQNADGGWGEDCRSYEDPRYVGLGPSTASQTA 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 588 WATDALIAVSSKPTAELQRGIRHLLTHNQA-NDWTTRyptgggrpggtYFA-----------YHSYRWIWPLLALSHYQA 655
Cdd:COG1657 573 WALLALLAAGEADSPAVARGIAYLLSTQREdGSWDEE-----------YFTgtgfprvfylrYHLYRQYFPLWALARYRN 641
|
...
gi 1371933383 656 KYA 658
Cdd:COG1657 642 LRG 644
|
|
| SQCY_1 |
cd02892 |
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ... |
36-653 |
1.74e-153 |
|
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: 457.43 E-value: 1.74e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 36 INRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLGI-HDEHLMEKLTAHITSLQHDNGAWKLYPDEHeGNLSTTI 114
Cdd:cd02892 1 IRRALEFLLSLQAPDGHWPGELEGPLFITAEYILLLYILGIpIDPEHRKEIARYLRNHQNPDGGWGLHHEGP-STMFGTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 115 DSYYALLLSGkYTKDEPRMALARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIALFLPSFPVSFYDFVGYAR 194
Cdd:cd02892 80 LNYVALRLLG-VSPDDPHMVKARNWILSHGGAARIPVWGKIWLALLGVYPWEGVPPLPPELWLLPSWLPFHPYKFWCWAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 195 VHLAPMMIVadrkYAKK---PDNAPDLS---DLYADTPISRGLYPHRfleNFLKEGQSFLASIHDSLQRL-----PFLPG 263
Cdd:cd02892 159 TVYVPMSYL----YGKRpvaPITPLVLSlrdELYVEPYEKINWYKHR---NDLYDYRPPWQRLFDALDRLlhwyePLPPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 264 QLHKLALRRLEQYILARIEPDGTLYNYSTSTFFMIFALLARGFsPKDPLIQKAMQGLSD-SVYVYENGAHLQLATSAVWD 342
Cdd:cd02892 232 PLRRKALRKAYEWILYRDENTGYLGIIPPPKANNMLALWVLGY-PDSPAFKRHLERIDDfLWLGPEGMKMCQTNGSQVWD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 343 TALLTSSLQKSGLST-THPAIQKANRYLLQKQ-QHTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTAALRSLRLLSRT 420
Cdd:cd02892 311 TALAVQALLEAGLAPeFDPALKKALDWLLESQiLDNPGDWKVKYRHLRKGGWAFSTANQGYPDSDDTAEALKALLRLQEL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 421 DITT----AAAWKRGLEWLLSMQNDDGGWPAFER-NTDADFIRQLPIEGADTVSTDPSSADLTGRTLEFLGNYA-----G 490
Cdd:cd02892 391 PPFGekvsRERLYDAVDWLLGMQNSNGGFAAFEPdNTYHWLENLNPFEDFGDIMIDPPYVECTGSVLEALGLFGklypgH 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 491 RTLTDPHVEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVG-FSPTDPAIQKAVAWLVANQNPDGGWGESCQS 569
Cdd:cd02892 471 RREIDPAIRRAVKYLLREQEPDGSWYGRWGVCYIYGTWFALEALAAAGeDYENSPYIRKACDFLLSKQNPDGGWGESYLS 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 570 DQKKTYVPLGASTPSQTAWATDALIAVSSKPTAELQRGIRHLLTHNQAN-DWttryptgggrpGGTYFA----------Y 638
Cdd:cd02892 551 YEDKSYAGGGRSTVVQTAWALLALMAAGEPDSEAVERGIKYLLNTQLPDgDW-----------PQEEITgvgfpnfyirY 619
|
650
....*....|....*
gi 1371933383 639 HSYRWIWPLLALSHY 653
Cdd:cd02892 620 HNYRNYFPLWALGRY 634
|
|
| hopene_cyclase |
TIGR01507 |
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ... |
31-658 |
1.95e-135 |
|
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: 411.20 E-value: 1.95e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 31 EVQQEINRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLGIHDEHLMEKLTAHITSLQHDNGAWKLYPDEhEGNL 110
Cdd:TIGR01507 13 RTVEAIDRAVDYLLSCQKDEGYWWGELESNVTIEAEYVLLCHILDRVDRDRMEKIRNYLLHEQREDGTWALYPGG-PGDL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 111 STTIDSYYALLLSGKyTKDEPRMALARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIALFLPSFPVSFYDFV 190
Cdd:TIGR01507 92 STTVEAYVALKYIGM-SRDEPPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWRGVPMVPPEIMLLPKRFPFNIYEFS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 191 GYARVHLAPMMIVADRKYAKKPDNAPDLSDLYA-DTPISRGLYPHrflenflkeGQSFLaSIHDSLQRL-----PFLPGQ 264
Cdd:TIGR01507 171 SWARATVVPLSIVCSRKPVFPLPERARVPELYEtDVPKPRRRGAK---------GGTGW-GIFDALDRAlhgyeKLSVHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 265 LHKLALRRLEQYILARIEPDGTLYNYSTSTFFMIFALLARGFSPKDPLIQKAMQGLSDSVYVYENGAHLQLATSAVWDTA 344
Cdd:TIGR01507 241 FRRAAEIRALDWLLERQAGDGSWGGIQPAMFNALIALKILGMTQHDAFIKLGWEGIDLYGVELDDSWMFQACVSPVWDTA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 345 LLTSSLQKSGLSTTHPAIQKANRYLLQKQQHTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTA---ALRSLRLLSrtD 421
Cdd:TIGR01507 321 LAVLALREAGLPADHDALVKAGEWLLDKQITVPGDWAVKRPNLEPGGWAFQFDNVYYPDVDDTAVvvwALNGLRLPD--E 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 422 ITTAAAWKRGLEWLLSMQNDDGGWPAFERNTDADFIRQLPIEGADTVsTDPSSADLTGRTLEFLGNYaGRTLTDPHVEKG 501
Cdd:TIGR01507 399 RRRRDAMTKAFRWIAGMQSSNGGWGAFDVDNTSDLLNHIPFCDFGAV-TDPPTADVTARVLECLGSF-GYDDAWPVIERA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 502 VRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVANQNPDGGWGESCQSDQKKTYVPLGAS 581
Cdd:TIGR01507 477 VEYLKREQEPDGSWFGRWGVNYLYGTGAVLSALKAVGIDTREPYIQKALAWLESHQNPDGGWGEDCRSYEDPAYAGKGAS 556
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371933383 582 TPSQTAWATDALIAVSSKPTAELQRGIRHLL-THNQANDWTTRYPTGGGRPGGTYFAYHSYRWIWPLLALSHY-QAKYA 658
Cdd:TIGR01507 557 TASQTAWALIALIAAGRAESEAARRGVQYLVeTQRPDGGWDEPYYTGTGFPGDFYLGYHMYRHVFPLLALARYkQAIER 635
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
36-655 |
1.55e-127 |
|
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: 390.26 E-value: 1.55e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 36 INRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLGIHDEHLMEKLTAHITSLQHDNGAWKLYPDEHeGNLSTTID 115
Cdd:TIGR01787 2 ARRAVEFLLSLQAPDGYWWGELEGPLTLLAEYVLLCHIADTPLPGYREKIVRYLRHHQNEDGGWGLHIGGK-STVFGTVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 116 SYYALLLSGKyTKDEPRMALARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIaLFLPSFpVSFYDFVGYARV 195
Cdd:TIGR01787 81 AYVALKILGM-SPDDPAMVRARNFILKQGGAVASPVFTKFWLALLGVYPWEGVPPLPPEI-MLLPKW-LPIHPSKSWCRC 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 196 HLAPMMIVadRKYAKKPDNAPDLSDLYADTPISrglyPHRFLENFLKEGQSFlasIHDSLQRL----------PFLPGQL 265
Cdd:TIGR01787 158 RMVYLPMS--YCYGERLSAPIDPREELYVEDDS----IRAQRNNVAKEDLYT---PHSWLLRAlygllnlfyhPFLRKAL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 266 HKLALRRLeqyiLARIEPDGTLynystSTFFMIFALLARGF--SPKDPLIQKAMQGLSDSVYVYENGAHLQLATSAVWDT 343
Cdd:TIGR01787 229 RKRALQWL----YEHIAADGSI-----GPISKAMAMLALWFldGPNSPAFQKHLQRIDDYLWLQLDGMKMQGTGSQVWDT 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 344 ALLTSSLQKSGLSTT---HPAIQKANRYLLQKQ--QHTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTA-ALRSLRLL 417
Cdd:TIGR01787 300 AFAIQALRESGDHRLpefHPALVKAHEWLLLSQipDNPPGDWKVYRHNLKPGGWAFSFLNCGYPDVDDTAVvALKAVLLL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 418 SRTDITTAAAWKRGLEWLLSMQNDDGGWPAFERNTDADFIRQL-PIEGADTVSTDPSSADLTGRTLEFLGNYAGRTLT-D 495
Cdd:TIGR01787 380 QEDEHVKRDRLRDAVNWILGMQSSNGGFAAYDPDNTGEWLELLnPSEVFGDIMIDPPYVDVTARVIQALGAFGHRADEiR 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 496 PHVEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVG-FSPTDPAIQKAVAWLVANQNPDGGWGESCQSDQKKT 574
Cdd:TIGR01787 460 NVLERALEYLRREQRADGSWFGRWGVNYTYGTGFVLSALAAAGrTYRNCPEVQKACDWLLSRQMPDGGWGEDCFSYEDPS 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 575 YVPLGASTPSQTAWATDALIAVSSKPTAELQRGIRHLLTHNQAN-DWTTRYPTGGGRPGGTYFAYHSYRWIWPLLALSHY 653
Cdd:TIGR01787 540 YVGSGGSTPSQTGWALMALIAAGEADSEAIERGVKYLLETQRPDgDWPQEYITGVGFPKNFYLKYTNYRNIFPLWALGRY 619
|
..
gi 1371933383 654 QA 655
Cdd:TIGR01787 620 RQ 621
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
337-654 |
1.31e-100 |
|
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: 310.04 E-value: 1.31e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 337 TSAVWDTALLTSSLQKSGLSTTHPAIQKANRYLLQKQQHTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTAALRSLRL 416
Cdd:pfam13243 1 VSPVWDTALALHALLEAGVPADHPALVKAAQWLLDRQVLVKGDWAVKRPDLEPGGWAFQFANDHYPDVDDTAVVVLALDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 417 LSRTDITTA-AAWKRGLEWLLSMQNDDGGWPAFERNTDADFIRQLPIEGADTVsTDPSSADLTGRTLEFLGNYaGRTLTD 495
Cdd:pfam13243 81 VRLPDERRRdDAIARGIEWILGMQSKNGGWGAFDKDNTKYYLNKIPFADHGAL-LDPPTADVTARVLEMLGQL-GYPDDH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 496 PHVEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVANQNPDGGWGESCQSDQKKTY 575
Cdd:pfam13243 159 PVAARALEYLKKEQEPDGSWFGRWGVNYIYGTWSVLCGLAAVGEDHNRPYIRKAVDWLKSRQNPDGGWGEDCESYKDPKL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 576 VPLGASTPSQTAWATDALIAVSSKPTAELQRGIRHLL-THNQANDWTTRYPTGGGRPGGTYFAYHSYRWIWPLLALSHYQ 654
Cdd:pfam13243 239 AGRGPSTASQTAWALLALMAAGEVDSPAVRRGIQYLLeTQKPDGTWDEPYFTGTGFPRVFYLKYHGYRNYFPLWALARYR 318
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
338-653 |
4.85e-99 |
|
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: 307.22 E-value: 4.85e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 338 SAVWDTALLTSSLQKSGLST-THPAIQKANRYLLQKQ-QHTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTAALRSLR 415
Cdd:cd02889 23 SQVWDTALALQALLEAGLAPeFDPALKKALEWLLKSQiRDNPDDWKVKYRHLRKGGWAFSTANQGYPDSDDTAEALKALL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 416 LLSRTDITT----AAAWKRGLEWLLSMQNDDGGWPAFERNTDADFIRqLPIEGADTVSTDPSSADLTGRTLEFLGnYAG- 490
Cdd:cd02889 103 RLQKKPPDGkkvsRERLYDAVDWLLSMQNSNGGFAAFEPDNTYKYLE-LIPEVDGDIMIDPPYVECTGSVLEALG-LFGk 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 491 -----RTLTDPHVEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVANQNPDGGWGE 565
Cdd:cd02889 181 lypehRREIDPAIRRAVKYLEREQEPDGSWYGRWGVCFIYGTWFALEALAAAGEDENSPYVRKACDWLLSKQNPDGGWGE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 566 SCQSDQKKTYVPLGASTPSQTAWATDALIAVSSKPTAELQRGIRHLLTHNQAN-DWttrYPTGGGRPGGTYFA--YHSYR 642
Cdd:cd02889 261 SYESYEDPSYAGGGRSTVVQTAWALLALMAAGEPDSEAVKRGVKYLLNTQQEDgDW---PQEEITGVFFKNFYirYHNYR 337
|
330
....*....|.
gi 1371933383 643 WIWPLLALSHY 653
Cdd:cd02889 338 NYFPLWALGRY 348
|
|
| SQHop_cyclase_N |
pfam13249 |
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
36-329 |
9.94e-94 |
|
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: 291.31 E-value: 9.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 36 INRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLGIHDEHLMEKLTAHITSLQHDNGAWKLYPDEHeGNLSTTID 115
Cdd:pfam13249 1 IARAQDALLSLQHPDGHWVGELEANVTITAEYILLRHFLGPDDPELEAKIARYLRSQQREDGGWPLFHGGP-GDLSTTVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 116 SYYALLLSGkYTKDEPRMALARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIALFLPSFPVSFYDFVGYARV 195
Cdd:pfam13249 80 AYFALKLLG-DSPDAPHMVRAREFILARGGAAKANVFTRIWLALFGQYPWRGVPSMPPEIMLLPRWFPFNIYKFSSWART 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 196 HLAPMMIVADRKYAKKPDNAPDLSDLYADTPISRGLYPHRFLENFLKegqSFLASIHDSLQRL-PFLPGQLHKLALRRLE 274
Cdd:pfam13249 159 TIVPLLILSALKPVAPLPPGIGLDELFVEPPENVRYYPRPHRLFSWT---NLFLGLDRVLKLYeRLPPKPLRRRALRKAE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1371933383 275 QYILARIEPDGTLYNYSTSTFFMIFALLARGFSPKDPLIQKAMQGLSDSVYVYEN 329
Cdd:pfam13249 236 EWILERQEGDGGLGGIFPAMVNSVLALHLLGYPLDHPVVARALEALDRLLVEDED 290
|
|
| squa_tetra_cyc |
TIGR04277 |
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, ... |
28-654 |
5.08e-52 |
|
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: 189.84 E-value: 5.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 28 ELREVQQEInRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLG-IHDEHLME-KLTAHITSLQHDNGAWKLYPDE 105
Cdd:TIGR04277 15 DIEEVQNAI-RDAQEICWAELHDNEWVYPPYLGELFISEYYFELKALGwIHKSAFEAsKFTEILLGSQFEDGSWEQVEDA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 106 H--EGNLSTTIDSYYALLLSGKYTKDEPRMALARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIALFLPSF- 182
Cdd:TIGR04277 94 NieTGQLDATIFNYWYLKAIGIDIHIDAALKKAQEWIKANGGIEAAQTMTKFKLAAFGQYPWEDLFKIPLFIFKKKGIFk 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 183 PVSFYDFVgyARVHLAPMMIVADRKYAKKPDNAP--DLSDLYADTP-----ISRGLYPHRFLENflkegqsflasihdsl 255
Cdd:TIGR04277 174 PLYIKDIT--AQWVYPHLTALAYLQNQRIIFNVAvaDIRELWINKAkkgikHQKKERPSFFIDN---------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 256 qrlpflpgqlhklALRRLEQYILARIEPDGTLYNYSTSTFFMIFALlaRGFSPKDP-----LIQKAMQGLSDSV----YV 326
Cdd:TIGR04277 236 -------------DLLILMDEIFKLKQPLGSFGAYTISTLLSLLAF--KDFQGKHPhkhknEIQDALEDGLDFVefnyFN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 327 YENGAHLQLATSAVWDTALLTSSLQKSGLST--THPAIQKANRYLLQkqqhtygdwkirnPKGKPG-GWGFSdyntMNPD 403
Cdd:TIGR04277 301 FREAYHGSLDDGRWWDTILISWAMLESGEDKekIFPIVENMLKEGLQ-------------PKGGIEyGYDFE----YAPD 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 404 IDDTTAALRslrLLSRTDITTAAAWKRGLEWLLSMQNDDGGWPAFERNTDAD---FIRQLPIEG-ADTVST-DPSSADLT 478
Cdd:TIGR04277 364 ADDTGLLLQ---VLSYYGEAFADAIDEGAEFLFSMQNDDGGFPAFDKGKMEDnllFKFAFKIAGiADSAEIfDPSCPDIT 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 479 GRTLEFLGNYAGRTlTDPHVEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVANQN 558
Cdd:TIGR04277 441 AHILEGLGEFGDQA-NHDQIQKMIKYFMDTQEKFGSWEARWGINYIMAAGAVLPALAKMNYDLNEGWAKNAINWLLNKQN 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 559 PDGGWGESCQS--DQKKtYVPLGASTPSQTAWATDALIAVSS-----KPTAELQRGIRHLLTHNQANDWTTRYPTGGGRP 631
Cdd:TIGR04277 520 ADGGFGECTLSynDPEK-WNGIGKSTVTQTSWGLLALLAVEDhndqiKEAADKAAQYLLDQFKRDDGEFKDHSTIGTGHR 598
|
650 660
....*....|....*....|...
gi 1371933383 632 GGTYFAYHSYRWIWPLLALSHYQ 654
Cdd:TIGR04277 599 GLLYLQYPSYAQSFPLIALGRFL 621
|
|
| osq_cycl |
TIGR03463 |
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ... |
43-653 |
3.42e-50 |
|
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: 184.81 E-value: 3.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 43 LLQRQQADGTWRFCLESSPMTDSHMIILLRTLG-IHDEHLMEKLTAHITSLQHDNGAWKLYPdEHEGNLSTTIDSYYALL 121
Cdd:TIGR03463 1 LAALQDSAGDWEGDMGGCQFIIAIAVAGLHVMGrPPDAEERAAIIAHFELHQLADGAWGLDP-EAPGQVFFSVLAYVALR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 122 LSGkYTKDEPRMALARSFIL-EKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIALFLPSFPVSFYDFVGYARVHLAPM 200
Cdd:TIGR03463 80 LLG-LGKDDAGLARARAWFHaQPEGPKASGAWGKFILALLGLYEREGLNAVPPELFLLPESLPFHPSRFWCHCRLIYLGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 201 MIVADRKyAKKPDNAPDL----SDLYAD--TPISRGLYPHRFLENFLKEGQSF-LASIHDSLQRLPFLPG-QLHKLALRR 272
Cdd:TIGR03463 159 AWLSGRG-ARAPESDPLLaairQEIFAEgyEQVDFGAARERVAPTDLFTPISFvLKAANDLLAGYERLAGkALRARALDF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 273 LEQYILAriEPDGTLYNYSTSTFFMIFALLARGFSPKDPLIQKAMQGLSDsvYVYENGA----HLQLATSAVWDTALLTS 348
Cdd:TIGR03463 238 AFEQILA--EDEATHYICIGPINGLLNCLAIFAHDPDGPDLAAHLEGLEA--WFWEDDAeglrMNGANSNALWDTAFAVQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 349 SLQKSG-LSTTHP-AIQKANRYLLQKQQ-HTYGDWK--IRNPKgkPGGWGFSDYNTMNPDIDDTTAALR-SLRLLSRTDI 422
Cdd:TIGR03463 314 ALAALGeLDEEAKhALEEAAAFIDAAQMlADLADPQeaFRDPA--KGGWCFSDGDHCWPISDCAAEALKaLFALEELGDN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 423 TT-----AAAWKRGLEWLLSMQNDDGGWPAFERNTDADFIRQL-PIEGADTVSTDPSSADLTGRTLEFLGNY-------- 488
Cdd:TIGR03463 392 RIsealgAARLQDAVEFILSMQNADGGFATYELQRGGKLLELLnPSDMFGQCMTDLSYVECTAACLGALAAWlkhhpdlp 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 489 AGRTltDPHVEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVANQNPDGGWGESCQ 568
Cdd:TIGR03463 472 DAKI--DAAIRKAEEFIRRRQLDDGSFMGFWGICFTYATFFGAKGLIAAGAEPADMALQAAAAFLLEKQRADGAWGEHVE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 569 SDQKKTYVPLGASTPSQTAWATDALIAVSSKPTAELQRGIRHLLTHNQANDWTTRYPTGGGRPGGTYFAYHSYRWIWPLL 648
Cdd:TIGR03463 550 SCLEARWVEGKHGHAVMTAWALLALAAAGEAAHDAAERGIAWLCEQQGEDGGWPPEGIAGIFFGAAAIDYDAYLRIFPTW 629
|
....*
gi 1371933383 649 ALSHY 653
Cdd:TIGR03463 630 ALARC 634
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
337-653 |
4.81e-40 |
|
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: 148.85 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 337 TSAVWDTALLTSSLQKSGLST-----THPAIQKANRYLLQKQQhtygdwkirnpkgKPGGWGFSDYNTmNPDIDDTTAAL 411
Cdd:cd00688 24 GEQTWSTAWPLLALLLLLAATgirdkADENIEKGIQRLLSYQL-------------SDGGFSGWGGND-YPSLWLTAYAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 412 RSLRLLSRTDITTAAAWKRGLEWLLSMQNDDGGWPAFERntdadfirqlpieGADTVSTDPSSADLTGRTLEFLGnYAGR 491
Cdd:cd00688 90 KALLLAGDYIAVDRIDLARALNWLLSLQNEDGGFREDGP-------------GNHRIGGDESDVRLTAYALIALA-LLGK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 492 TLTDPHVEKGVRWLLNHQEANGSWyGRWGIAYLYGTWAAITGLMAVGfSPTDPAIQKAVAWLVANQNPDGGWGESCQSDQ 571
Cdd:cd00688 156 LDPDPLIEKALDYLLSCQNYDGGF-GPGGESHGYGTACAAAALALLG-DLDSPDAKKALRWLLSRQRPDGGWGEGRDRTN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 572 KKtyvplgaSTPSQTAWATDALIA-VSSKPTAELQRGIRHLLTHNQAN-DWTTRYPTGggrpggtyfaYHSYRWIWPLLA 649
Cdd:cd00688 234 KL-------SDSCYTEWAAYALLAlGKLGDLEDAEKLVKWLLSQQNEDgGFSSKPGKS----------YDTQHTVFALLA 296
|
....
gi 1371933383 650 LSHY 653
Cdd:cd00688 297 LSLY 300
|
|
| PLN02993 |
PLN02993 |
lupeol synthase |
35-654 |
5.59e-39 |
|
lupeol synthase
Pssm-ID: 215537 [Multi-domain] Cd Length: 763 Bit Score: 153.91 E-value: 5.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 35 EINRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLG----IHDEHLMEKLTAHITSLQHDNGAWKLYPdEHEGNL 110
Cdd:PLN02993 98 ALRRGVSFFSALQASDGHWPGEITGPLFFLPPLVFCLYITGhleeVFDAEHRKEMLRHIYCHQNEDGGWGLHI-ESKSVM 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 111 STTIDSYYALLLSGKYTKDEPRMAL--ARSFILEKGGLTHANMLTKFSTALTGQYQWPSHFLVPVEIaLFLPSF-PVSFY 187
Cdd:PLN02993 177 FCTVLNYICLRMLGEGPNGGRENACkrARQWILDHGGVTYIPSWGKFWLSILGIYDWSGTNPMPPEI-WLLPSFlPIHLG 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 188 DFVGYARVHLAPMMIVADRKYAK------------------KPDNAPDLSDLYADTPIsrgLYPHRFLENFLKEgqsfla 249
Cdd:PLN02993 256 KTLCYTRMVYMPMSYLYGKRFVGpitplimllreelhlqpyEEINWNKARRLCAKEDM---YYPHPLVQDLIWD------ 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 250 SIHDSLQrlPFLPG-QLHKLALRRLEQYILARIEPDGTLYNYST-STFFMIFALLARGF-SPKDPLIQKAMQGLSDSVYV 326
Cdd:PLN02993 327 TLHNFVE--PFLTRwPLNKLVREKALQVAMKHIHYEDENSHYITiGCVEKVLCMLACWIeNPNGDHFKKHLARIPDYMWV 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 327 YENGAHLQLATSAVWDTALLTSSLQKSGLS-TTHPAIQKANRYLLQKQ--QHTYGDWKIRNPKGKPGGWGFSDYNTMNPD 403
Cdd:PLN02993 405 AEDGMKMQSFGSQLWDTGFAIQALLASDLSdETDDVLRRGHNYIKKSQvrENPSGDFKSMYRHISKGAWTLSDRDHGWQV 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 404 IDDTTAALRSLRLLSR--TDITTAAAWKRGL----EWLLSMQNDDGGWPAFERNTDADFIRQL-PIEGADTVSTDPSSAD 476
Cdd:PLN02993 485 SDCTAEALKCCMLLSMmpADVVGQKIDPEQLydsvNLLLSLQSENGGVTAWEPVRAYKWLELLnPTDFFANTMVEREYVE 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 477 LTGRTLEFLGNYagRTLTDPH--------VEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDP-AIQ 547
Cdd:PLN02993 565 CTSAVIQALVLF--KQLYPDHrtkeiiksIEKAVQFIESKQTPDGSWYGNWGICFIYATWFALGGLAAAGKTYNDClAMR 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 548 KAVAWLVANQNPDGGWGESCQSDQKKTYVPLGA--STPSQTAWATDALIAV--SSKPTAELQRGIRHLLTHNQANDWTTR 623
Cdd:PLN02993 643 KGVHFLLTIQRDDGGWGESYLSCPEQRYIPLEGnrSNLVQTAWAMMGLIHAgqAERDLIPLHRAAKLIITSQLENGDFPQ 722
|
650 660 670
....*....|....*....|....*....|.
gi 1371933383 624 YPTGGGRPGGTYFAYHSYRWIWPLLALSHYQ 654
Cdd:PLN02993 723 QEILGAFMNTCMLHYATYRNTFPLWALAEYR 753
|
|
| PLN03012 |
PLN03012 |
Camelliol C synthase |
79-656 |
1.31e-36 |
|
Camelliol C synthase
Pssm-ID: 166653 [Multi-domain] Cd Length: 759 Bit Score: 146.70 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 79 EHLMEKLTaHITSLQHDNGAWKLYPDEHEGNLSTTIDsYYALLLSGKYTKDEPRMAL--ARSFILEKGGLTHANMLTKFS 156
Cdd:PLN03012 147 DHRKEILR-YIYCHQKEDGGWGLHIEGHSTMFCTTLN-YICMRILGEGPDGGHDNACgrARDWILDHGGATYIPSWGKTW 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 157 TALTGQYQWPSHFLVPVEIALfLPSF-PVSFYDFVGYARVHLAPMMIVADRKYAKkPDNAPDLS---DLYADtPISR--- 229
Cdd:PLN03012 225 LSILGVFDWSGSNPMPPEFWI-LPSFfPIHPAKMWCYCRLVYLPMSYLYGKRFVG-PISPLILQlreEIYLQ-PYAEinw 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 230 -----------GLYPHRFLENFLKEGQSFLAsiHDSLQRLPFlpgqlHKLALRRLEQYILARIEpdgtlYNYSTSTFFMI 298
Cdd:PLN03012 302 mkarhlcakedAYCPHPLIQDLIWDCLYIFA--EPFLACWPF-----NKLLREKALGLAMKHIH-----YEDENSRYITI 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 299 ------FALLARGFS-PKDPLIQKAMQGLSDSVYVYENGAHLQLATSAVWDTALLTSSLQKSGLSTTHPAIQKANRYLLQ 371
Cdd:PLN03012 370 gcvekaLCMLACWVEdPNGDHFKKHLLRISDYLWIAEDGMKMQSFGSQLWDSGFALQALLASNLSNEIPDVLRRGHDFIK 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 372 KQQ---HTYGDWKIRNPKGKPGGWGFSDYNTMNPDIDDTTAALRSLRLLSRT--DIT----TAAAWKRGLEWLLSMQNDD 442
Cdd:PLN03012 450 NSQvgeNPSGDFKNMYRHISKGAWTFSDRDHGWQASDCTAEGFKCCLLFSMIapDIVgpkmDPEQLHDAVNILLSLQSKN 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 443 GGWPAFERNTDADFIRQL-PIEGADTVSTDPSSADLTGRTLEFLGNYagRTLTDPH--------VEKGVRWLLNHQEANG 513
Cdd:PLN03012 530 GGMTAWEPAGAPEWLELLnPTEMFADIVIEHEYNECTSSAIQALILF--KQLYPDHrteeinafIKKAAEYIENIQMLDG 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 514 SWYGRWGIAYLYGTWAAITGLMAVGFSPTD-PAIQKAVAWLVANQNPDGGWGESCQSDQKKTYVPLGA--STPSQTAWAT 590
Cdd:PLN03012 608 SWYGNWGICFTYGTWFALAGLAAAGKTFNDcEAIRKGVHFLLAAQKDNGGWGESYLSCPKKIYIAQEGeiSNLVQTAWAL 687
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1371933383 591 DALI--AVSSKPTAELQRGIRHLLTHNQANDWTTRYPTGGGRPGGTYFAYHSYRWIWPLLALSHYQAK 656
Cdd:PLN03012 688 MGLIhaGQAERDPIPLHRAAKLIINSQLENGDFPQQEATGAFLKNCLLHYAAYRNIFPLWALAEYRAR 755
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
363-602 |
5.04e-08 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 54.73 E-value: 5.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 363 QKANRYLLQKQqhtygdwkirNPKGkpggwGFSDYNTMNPDIDDTTAALRSLRLL----SRTDITtaaawkrgLEWLLSM 438
Cdd:COG1689 9 ARTIEYVLKRQ----------NEDG-----GFCAYPGLPSTLADTYYAVRILKLLgeevPNRDKT--------IEFLESC 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 439 QNDDGGwpAFERNTDADFIRQLPIEGADTVSTDPSSADLTGRTLEFLGN---------YAGRTLT-----DPHVEKGVRW 504
Cdd:COG1689 66 QDEEGG--GFALYTTSYGLMALALLGIDPPDEQEALEYLSDALPTKFAGgasdleetyLAVALLEalgasEPEREKIREF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 505 LLNHQEANGSwYGRwGIAYLYGTWAAITGLMAVGFSPTDPaiQKAVAWLVANQNPDGGWgescqsdqkkTYVPLGASTPS 584
Cdd:COG1689 144 LLSLRRPDGG-FGG-KKPNLEDTYWALAALRRLGRDLPPA--DRVIAFILACQNEDGGF----------SKTPGSYSDLE 209
|
250
....*....|....*...
gi 1371933383 585 QTAWATDALIAVSSKPTA 602
Cdd:COG1689 210 ATYYALRALKLLGEPPKN 227
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
496-538 |
9.64e-08 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 48.66 E-value: 9.64e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1371933383 496 PHVEKGVRWLLNHQEANGSWYGRWG-IAYLYGTWAAITGLMAVG 538
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGgESDTYYTYCALAALALLG 44
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
265-446 |
1.37e-07 |
|
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: 53.71 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 265 LHKLALRRLEQYILARIEPDGTL-------------YNYSTSTFFMIFALLARGFSPKDPLIQKAMQglsdsvYVYEN-- 329
Cdd:cd00688 101 VDRIDLARALNWLLSLQNEDGGFredgpgnhriggdESDVRLTAYALIALALLGKLDPDPLIEKALD------YLLSCqn 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 330 --GAHLQLATSAVWDTALLTSSLQKSGlSTTHPAIQKANRYLLQKQQHTYGDWKIRNPKGKPggwgfsdyntmnPDIDDT 407
Cdd:cd00688 175 ydGGFGPGGESHGYGTACAAAALALLG-DLDSPDAKKALRWLLSRQRPDGGWGEGRDRTNKL------------SDSCYT 241
|
170 180 190
....*....|....*....|....*....|....*....
gi 1371933383 408 TAALRSLRLLSRTDITTAAawKRGLEWLLSMQNDDGGWP 446
Cdd:cd00688 242 EWAAYALLALGKLGDLEDA--EKLVKWLLSQQNEDGGFS 278
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
413-580 |
1.55e-06 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 50.09 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 413 SLRLLSRTDiTTAAAW-----KRGLEWLLSMQNDDGGWPafERNTDADFirqlpiegadtvstdpSSADLTGRTLEFLGn 487
Cdd:COG5029 2 SLGVLSRLE-GGSSKStadftDSHLDYLRASQNPDGGFA--GRSGPSDL----------------YSTYYAVRTLALLG- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 488 yagrtLTDPHVEKGVRWLLNHQEANGSwYGR---WGIAYLYGTWAAITGLMAVGFSPTDPaiQKAVAWLVANQNPDGGWG 564
Cdd:COG5029 62 -----ESPKWRDRVADLLSSLRVEDGG-FAKapeGGAGSTYHTYLATLLAELLGRPPPDP--DRLVRFLISQQNDDGGFE 133
|
170
....*....|....*...
gi 1371933383 565 --ESCQSDQKKTYVPLGA 580
Cdd:COG5029 134 isPGRRSDTNPTAAAIGA 151
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
269-381 |
1.08e-05 |
|
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.
Pssm-ID: 239219 [Multi-domain] Cd Length: 348 Bit Score: 47.98 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 269 ALRRLEQYILARIEPDGTLY-----NYSTSTFFMIFALLARGFSPKDPLIQKAMQGL----------SDSVYVYENGAHL 333
Cdd:cd02889 192 AIRRAVKYLEREQEPDGSWYgrwgvCFIYGTWFALEALAAAGEDENSPYVRKACDWLlskqnpdggwGESYESYEDPSYA 271
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1371933383 334 QLATSAVWDTALLTSSLQKSGlSTTHPAIQKANRYLLQKQQHTyGDWK 381
Cdd:cd02889 272 GGGRSTVVQTAWALLALMAAG-EPDSEAVKRGVKYLLNTQQED-GDWP 317
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
10-143 |
7.67e-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: 45.23 E-value: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 10 SMLFPLSSLgDVFYREVNELREVQQEINRIQAFLLQRQQADGTWRFCLES-SPMTDS-----HMIILLRTLGIHDEHLME 83
Cdd:cd00688 29 STAWPLLAL-LLLLAATGIRDKADENIEKGIQRLLSYQLSDGGFSGWGGNdYPSLWLtayalKALLLAGDYIAVDRIDLA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933383 84 KLTAHITSLQHDNGAWKLYPDEHEGNLSTTID---SYYA---LLLSGKYTKDEPrMALARSFILEK 143
Cdd:cd00688 108 RALNWLLSLQNEDGGFREDGPGNHRIGGDESDvrlTAYAliaLALLGKLDPDPL-IEKALDYLLSC 172
|
|
| complement_C3_C4_C5 |
cd02896 |
Proteins similar to C3, C4 and C5 of vertebrate complement. The vertebrate complement system, ... |
497-568 |
2.99e-04 |
|
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: 43.42 E-value: 2.99e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1371933383 497 HVEKGVRWLLNHQEANGSwYGRWGiAYLYGTWaaITGL------MAVGFSPTDP-AIQKAVAWLVANQNPDGGWGESCQ 568
Cdd:cd02896 53 YIRQGYQRQLSYRKPDGS-YAAWK-NRPSSTW--LTAFvvkvfsLARKYIPVDQnVICGSVNWLISNQKPDGSFQEPSP 127
|
|
| SQHop_cyclase_N |
pfam13249 |
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
450-551 |
4.09e-04 |
|
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: 42.86 E-value: 4.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 450 RNTDADFIRQLPIEGADTVSTDPSSADLTG---------RTLEFLGNYAGRTLTDPHVEKGVRWLLNHQEANGSWYGRWg 520
Cdd:pfam13249 174 PLPPGIGLDELFVEPPENVRYYPRPHRLFSwtnlflgldRVLKLYERLPPKPLRRRALRKAEEWILERQEGDGGLGGIF- 252
|
90 100 110
....*....|....*....|....*....|.
gi 1371933383 521 IAYLYgtwaAITGLMAVGFSPTDPAIQKAVA 551
Cdd:pfam13249 253 PAMVN----SVLALHLLGYPLDHPVVARALE 279
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
498-618 |
4.60e-04 |
|
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: 42.54 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 498 VEKGVRWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGF-----SPTDPAIQKAVAWLVANQNPDGGWGescqsdqk 572
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAatgirDKADENIEKGIQRLLSYQLSDGGFS-------- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1371933383 573 ktyVPLGASTPSQ--TAWATDALIAVSSKPTAE---LQRGIRHLLTHNQAN 618
Cdd:cd00688 73 ---GWGGNDYPSLwlTAYALKALLLAGDYIAVDridLARALNWLLSLQNED 120
|
|
| SQHop_cyclase_N |
pfam13249 |
Squalene-hopene cyclase N-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
429-556 |
7.76e-04 |
|
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: 42.09 E-value: 7.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 429 KRGLEWLLSMQNDDGGWPA-FERNT--DADFI--RQlpiegadtvstdpssadltgrtleFLGnyagrTLTDPHVEKGVR 503
Cdd:pfam13249 2 ARAQDALLSLQHPDGHWVGeLEANVtiTAEYIllRH------------------------FLG-----PDDPELEAKIAR 52
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933383 504 WLLNHQEANGSW---YGrwGIAYLYGTWAAITGLMAVGFSPTDPAIQKAVAWLVAN 556
Cdd:pfam13249 53 YLRSQQREDGGWplfHG--GPGDLSTTVEAYFALKLLGDSPDAPHMVRAREFILAR 106
|
|
| A2M_like |
cd02891 |
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
431-556 |
8.03e-04 |
|
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier protein in serum. It is a broadly specific proteinase inhibitor. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. This group contains another broadly specific proteinase inhibitor: pregnancy zone protein (PZP). PZP is a trace protein in the plasma of non-pregnant females and males which is elevated in pregnancy. Alpha (2)-M and PZ bind to placental protein-14 and may modulate its activity in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system. This group also contains C3, C4 and C5 of vertebrate complement. The vertebrate complement is an effector of both the acquired and innate immune systems The point of convergence of the classical, alternative and lectin pathways of the complement system is the proteolytic activation of C3. C4 plays a key role in propagating the classical and lectin pathways. C5 participates in the classical and alternative pathways. The thioester bond located within the structure of C3 and C4 is central to the function of complement. C5 does not contain an active thioester bond.
Pssm-ID: 239221 [Multi-domain] Cd Length: 282 Bit Score: 41.99 E-value: 8.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 431 GLEWLLSMQNDDGGWPAFErntdadfirqlpiegadtvSTDPSSADLTGRTLEFLGNYAGRTLTDPHVE-KGVRWLLNHQ 509
Cdd:cd02891 54 GYQRLLTYQRSDGSFSAWG-------------------NSDSGSTWLTAYVVKFLSQARKYIDVDENVLaRALGWLVPQQ 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1371933383 510 EANGSWYGRWGIAY---LYGTW------AAITGLMAVGFSPTDPAIQKAVAWLVAN 556
Cdd:cd02891 115 KEDGSFRELGPVIHremKGGVDdsvsltAYVLIALAEAGKACDASIEKALAYLETQ 170
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
36-141 |
1.38e-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: 41.38 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 36 INRIQAFLLQRQQADGTWRFCLESSPMTD-----SHMIILLRTLGIHDEHL--MEKLTAHITSLQHDNGAWKLYPDEHEG 108
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWStawplLALLLLLAATGIRDKADenIEKGIQRLLSYQLSDGGFSGWGGNDYP 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1371933383 109 NLSTTidsYYAL----LLSGKYTKDEPRMALARSFIL 141
Cdd:cd00688 81 SLWLT---AYALkallLAGDYIAVDRIDLARALNWLL 114
|
|
| A2M_like |
cd02891 |
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ... |
497-593 |
2.27e-03 |
|
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: 40.45 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 497 HVEKGVRWLLNHQEANGSwYGRWGIAYLYGTWaaITG------LMAVGFSPTDP-AIQKAVAWLVANQNPDGGWGESCQS 569
Cdd:cd02891 50 YIRKGYQRLLTYQRSDGS-FSAWGNSDSGSTW--LTAyvvkflSQARKYIDVDEnVLARALGWLVPQQKEDGSFRELGPV 126
|
90 100
....*....|....*....|....
gi 1371933383 570 DQKKTyVPLGASTPSQTAWATDAL 593
Cdd:cd02891 127 IHREM-KGGVDDSVSLTAYVLIAL 149
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
503-587 |
2.35e-03 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 40.46 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 503 RWLLNHQEANGSWYGRWGIAYLYGTWAAITGLMAVGFSPTDPaiQKAVAWLVANQNPDGGWGESCQSDQKKTY------- 575
Cdd:COG5029 26 DYLRASQNPDGGFAGRSGPSDLYSTYYAVRTLALLGESPKWR--DRVADLLSSLRVEDGGFAKAPEGGAGSTYhtylatl 103
|
90
....*....|....
gi 1371933383 576 --VPLGASTPSQTA 587
Cdd:COG5029 104 laELLGRPPPDPDR 117
|
|
| SQHop_cyclase_C |
pfam13243 |
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ... |
269-381 |
5.50e-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: 39.24 E-value: 5.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 269 ALRRLEQYILARIEPDGTLY-----NYSTSTFFMIFALLARGFSPKDPLIQKAMQ----------GLSDSVYVYENGAHL 333
Cdd:pfam13243 160 VAARALEYLKKEQEPDGSWFgrwgvNYIYGTWSVLCGLAAVGEDHNRPYIRKAVDwlksrqnpdgGWGEDCESYKDPKLA 239
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1371933383 334 QLATSAVWDTALLTSSLQKSGLStTHPAIQKANRYLLQKQQHTyGDWK 381
Cdd:pfam13243 240 GRGPSTASQTAWALLALMAAGEV-DSPAVRRGIQYLLETQKPD-GTWD 285
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
36-142 |
5.55e-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: 5.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1371933383 36 INRIQAFLLQRQQADGTWRFCLESSPMTDSHMIILLRTLGIHDEHLMEKLTAHITSLQHDNGAWKLYPDEHeGNLSTTID 115
Cdd:cd00688 162 IEKALDYLLSCQNYDGGFGPGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDRT-NKLSDSCY 240
|
90 100 110
....*....|....*....|....*....|
gi 1371933383 116 SY---YALLLSGKYTKDEPRMALARsFILE 142
Cdd:cd00688 241 TEwaaYALLALGKLGDLEDAEKLVK-WLLS 269
|
|
| |
