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Conserved domains on  [gi|15219383|ref|NP_178064|]
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Terpenoid cyclases/Protein prenyltransferases superfamily protein [Arabidopsis thaliana]

Protein Classification

PLN02279 family protein( domain architecture ID 11476593)

PLN02279 family protein

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02279 PLN02279
ent-kaur-16-ene synthase
1-785 0e+00

ent-kaur-16-ene synthase


:

Pssm-ID: 177918 [Multi-domain]  Cd Length: 784  Bit Score: 1420.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383    1 MSINLRSSGCSSPISATLERRLDSEVQTRANNVSFEQTKEKIRKMLEKVELSVSAYDTSWVAMVPSPSSQNAPLFPQCVK 80
Cdd:PLN02279   1 MSINLRSSGCSSPISATLEPRLKTWTQTRANNVSFEGTKERIKKMFDKVELSVSSYDTAWVAMVPSPNSQQAPLFPECVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   81 WLLDNQHEDGSWGLDnHDHQSLKKDVLSSTLASILALKKWGIGERQINKGLQFIELNSALVTDETIQKPTGFDIIFPGMI 160
Cdd:PLN02279  81 WLLENQLEDGSWGLP-HDHPLLVKDALSSTLASILALKKWGVGEEQINKGLQFIELNSASVTDEKQHKPIGFDIIFPGMI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  161 KYARDLNLTIPLGSEVVDDMIRKRDLDLKCDSEKFSKGREAYLAYVLEGTRNLKDWDLIVKYQRKNGSLFDSPATTAAAF 240
Cdd:PLN02279 160 EYAKDLDLNLPLGSEVVDAMLHKRDLDLKSGGGSNTKGREAYLAYVSEGIGKLQDWEMVMKYQRKNGSLFNSPSTTAAAF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  241 TQFGNDGCLRYLCSLLQKFEAAVPSVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCA 320
Cdd:PLN02279 240 SHLQNAGCLRYLRSLLQKFGNAVPTVYPLDQYARLSMVDTLERLGIDRHFRKEIKSVLDETYRYWLQGEEEIFLDLATCA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  321 LAFRLLLAHGYDVSYDPLKPFAEESgFSDTLEGYVKNTFSVLELFKAAQ-SYPHESALKKQCCWTKQYLEMELSSWVKTS 399
Cdd:PLN02279 320 LAFRILRLNGYDVSSDPLKQFAEDH-FSDSLGGYLKDTGAVLELFRASQiSYPDESLLEKQNSWTSHFLEQGLSNWSKTA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  400 VR-DKYLKKEVEDALAFPSYASLERSDHRRKILNgSAVENTRVTKTSYRLHNICTSDILKLAVDDFNFCQSIHREEMERL 478
Cdd:PLN02279 399 DRlRKYIKKEVEDALNFPYYANLERLANRRSIEN-YAVDDTRILKTSYRCSNICNQDFLKLAVEDFNFCQSIHREELKQL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  479 DRWIVENRLQELKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLNGV 558
Cdd:PLN02279 478 ERWIVENRLDKLKFARQKLAYCYFSAAATLFSPELSDARLSWAKNGVLTTVVDDFFDVGGSEEELENLIQLVEKWDVNGS 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  559 PEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPI 638
Cdd:PLN02279 558 PDFCSEQVEIIFSALRSTISEIGDKAFTWQGRNVTSHIIKIWLDLLKSMLTEAQWSSNKSTPTLDEYMTNAYVSFALGPI 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  639 VLPATYLIGPPLPEKTVDSHQYNQLYKLVSTMGRLLNDIQGFKRESAEGKLNAVSLHMKHERDNRSKEVIIESMKGLAER 718
Cdd:PLN02279 638 VLPALYLVGPKLSEEVVDSPELHKLYKLMSTCGRLLNDIRGFKRESKEGKLNAVSLHMIHGNGNSTEEEAIESMKGLIES 717
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219383  719 KREELHKLVLEEKGSVVPRECKEAFLKMSKVLNLFYRKDDGFTSNDLMSLVKSVIYEPVSLQEESLT 785
Cdd:PLN02279 718 QRRELLRLVLQEKGSNVPRECKDLFWKMSKVLHLFYRKDDGFTSNDMMSLVKSVIYEPVSLQEESLT 784
 
Name Accession Description Interval E-value
PLN02279 PLN02279
ent-kaur-16-ene synthase
1-785 0e+00

ent-kaur-16-ene synthase


Pssm-ID: 177918 [Multi-domain]  Cd Length: 784  Bit Score: 1420.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383    1 MSINLRSSGCSSPISATLERRLDSEVQTRANNVSFEQTKEKIRKMLEKVELSVSAYDTSWVAMVPSPSSQNAPLFPQCVK 80
Cdd:PLN02279   1 MSINLRSSGCSSPISATLEPRLKTWTQTRANNVSFEGTKERIKKMFDKVELSVSSYDTAWVAMVPSPNSQQAPLFPECVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   81 WLLDNQHEDGSWGLDnHDHQSLKKDVLSSTLASILALKKWGIGERQINKGLQFIELNSALVTDETIQKPTGFDIIFPGMI 160
Cdd:PLN02279  81 WLLENQLEDGSWGLP-HDHPLLVKDALSSTLASILALKKWGVGEEQINKGLQFIELNSASVTDEKQHKPIGFDIIFPGMI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  161 KYARDLNLTIPLGSEVVDDMIRKRDLDLKCDSEKFSKGREAYLAYVLEGTRNLKDWDLIVKYQRKNGSLFDSPATTAAAF 240
Cdd:PLN02279 160 EYAKDLDLNLPLGSEVVDAMLHKRDLDLKSGGGSNTKGREAYLAYVSEGIGKLQDWEMVMKYQRKNGSLFNSPSTTAAAF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  241 TQFGNDGCLRYLCSLLQKFEAAVPSVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCA 320
Cdd:PLN02279 240 SHLQNAGCLRYLRSLLQKFGNAVPTVYPLDQYARLSMVDTLERLGIDRHFRKEIKSVLDETYRYWLQGEEEIFLDLATCA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  321 LAFRLLLAHGYDVSYDPLKPFAEESgFSDTLEGYVKNTFSVLELFKAAQ-SYPHESALKKQCCWTKQYLEMELSSWVKTS 399
Cdd:PLN02279 320 LAFRILRLNGYDVSSDPLKQFAEDH-FSDSLGGYLKDTGAVLELFRASQiSYPDESLLEKQNSWTSHFLEQGLSNWSKTA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  400 VR-DKYLKKEVEDALAFPSYASLERSDHRRKILNgSAVENTRVTKTSYRLHNICTSDILKLAVDDFNFCQSIHREEMERL 478
Cdd:PLN02279 399 DRlRKYIKKEVEDALNFPYYANLERLANRRSIEN-YAVDDTRILKTSYRCSNICNQDFLKLAVEDFNFCQSIHREELKQL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  479 DRWIVENRLQELKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLNGV 558
Cdd:PLN02279 478 ERWIVENRLDKLKFARQKLAYCYFSAAATLFSPELSDARLSWAKNGVLTTVVDDFFDVGGSEEELENLIQLVEKWDVNGS 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  559 PEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPI 638
Cdd:PLN02279 558 PDFCSEQVEIIFSALRSTISEIGDKAFTWQGRNVTSHIIKIWLDLLKSMLTEAQWSSNKSTPTLDEYMTNAYVSFALGPI 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  639 VLPATYLIGPPLPEKTVDSHQYNQLYKLVSTMGRLLNDIQGFKRESAEGKLNAVSLHMKHERDNRSKEVIIESMKGLAER 718
Cdd:PLN02279 638 VLPALYLVGPKLSEEVVDSPELHKLYKLMSTCGRLLNDIRGFKRESKEGKLNAVSLHMIHGNGNSTEEEAIESMKGLIES 717
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219383  719 KREELHKLVLEEKGSVVPRECKEAFLKMSKVLNLFYRKDDGFTSNDLMSLVKSVIYEPVSLQEESLT 785
Cdd:PLN02279 718 QRRELLRLVLQEKGSNVPRECKDLFWKMSKVLHLFYRKDDGFTSNDMMSLVKSVIYEPVSLQEESLT 784
Terpene_cyclase_plant_C1 cd00684
Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene ...
265-776 4.07e-178

Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene cyclases (Tspa-Tspf) that convert the acyclic isoprenoid diphosphates, geranyl diphosphate (GPP), farnesyl diphosphate (FPP), or geranylgeranyl diphosphate (GGPP) into cyclic monoterpenes, diterpenes, or sesquiterpenes, respectively; a few form acyclic species. Terpnoid cyclases are soluble enzymes localized to the cytosol (sesquiterpene synthases) or plastids (mono- and diterpene synthases). All monoterpene and diterpene synthases have restrict substrate specificity, however, some sesquiterpene synthases can accept both FPP and GPP. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl diphosphates, via bridging Mg2+ ions (K+ preferred by gymnosperm cyclases), inducing conformational changes such that an N-terminal region forms a cap over the catalytic core. Loss of diphosphate from the enzyme-bound substrate (GPP, FPP, or GGPP) results in an allylic carbocation that electrophilically attacks a double bond further down the terpene chain to effect the first ring closure. Unlike monoterpene, sesquiterene, and macrocyclic diterpenes synthases, which undergo substrate ionization by diphosphate ester scission, Tpsc-like diterpene synthases catalyze cyclization reactions by an initial protonation step producing a copalyl diphosphate intermediate. These enzymes lack the aspartate-rich sequences mentioned above. Most diterpene synthases have an N-terminal, internal element (approx 210 aa) whose function is unknown.


Pssm-ID: 173832 [Multi-domain]  Cd Length: 542  Bit Score: 521.76  E-value: 4.07e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 265 SVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCALAFRLLLAHGYDVSYDPLKPFAEE 344
Cdd:cd00684  47 SEYPVDLFERLWLIDRLQRLGISYHFEDEIKEILDYIYRYWTERGESNEDDLYTTALGFRLLRQHGYNVSSDVFKKFKDE 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 345 SG-FSDTLegyVKNTFSVLELFKAAQ-SYPHESALKKQCCWTKQYLEMELSSWvktSVRDKYLKKEVEDALAFPSYASLE 422
Cdd:cd00684 127 DGkFKESL---TQDVKGMLSLYEASHlSFPGEDILDEALSFTTKHLEEKLESN---WIIDPDLSGEIEYALEIPLHASLP 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 423 RSDHRRKILNGSAVENtrvtktsyrlHNictSDILKLAVDDFNFCQSIHREEMERLDRWIVENRLQE-LKFARQKLAYCY 501
Cdd:cd00684 201 RLEARWYIEFYEQEDD----------HN---ETLLELAKLDFNILQALHQEELKILSRWWKDLDLASkLPFARDRLVECY 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 502 FSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLNGVpEYSSEHVEIIFSVLRDTILETG 581
Cdd:cd00684 268 FWAAGTYFEPQYSLARIALAKTIALITVIDDTYDVYGTLEELELFTEAVERWDISAI-DQLPEYMKIVFKALLNTVNEIE 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 582 DKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPIVLPATYLIGPPLPEKTVDSHQYN 661
Cdd:cd00684 347 EELLKEGGSYVVPYLKEAWKDLVKAYLVEAKWAHEGYVPTFEEYMENALVSIGLGPLLLTSFLGMGDILTEEAFEWLESR 426
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 662 Q-LYKLVSTMGRLLNDIQGFKRESAEGK-LNAVSLHMKHErdNRSKEVIIESMKGLAERKREELHKLVLEEKgSVVPREC 739
Cdd:cd00684 427 PkLVRASSTIGRLMNDIATYEDEMKRGDvASSIECYMKEY--GVSEEEAREEIKKMIEDAWKELNEEFLKPS-SDVPRPI 503
                       490       500       510
                ....*....|....*....|....*....|....*....
gi 15219383 740 KEAFLKMSKVLNLFYRKDDGFTSND--LMSLVKSVIYEP 776
Cdd:cd00684 504 KQRFLNLARVIDVFYKEGDGFTHPEgeIKDHITSLLFEP 542
Terpene_synth_C pfam03936
Terpene synthase family, metal binding domain; It has been suggested that this gene family be ...
457-722 1.64e-94

Terpene synthase family, metal binding domain; It has been suggested that this gene family be designated tps (for terpene synthase). It has been split into six subgroups on the basis of phylogeny, called tpsa-tpsf. tpsa includes vetispiridiene synthase, 5-epi- aristolochene synthase, and (+)-delta-cadinene synthase. tpsb includes (-)-limonene synthase. tpsc includes kaurene synthase A. tpsd includes taxadiene synthase, pinene synthase, and myrcene synthase. tpse includes kaurene synthase B. tpsf includes linalool synthase.


Pssm-ID: 461096 [Multi-domain]  Cd Length: 266  Bit Score: 295.59  E-value: 1.64e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   457 LKLAVDDFNFCQSIHREEMERLDRWIVENRLQE-LKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFD 535
Cdd:pfam03936   1 LELAKLDFNLLQSLHQKELKELTRWWKELGLASkLPFARDRLVECYFWALGVYFEPQYSRARIILAKVIVLITIIDDTYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   536 VGGSKEELENLIHLVEKWDLNGVpEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSS 615
Cdd:pfam03936  81 VYGTLEELELLTEAVERWDESAI-EQLPEYMKICFKALLNTFNEIEEELSKGKGYNVIPYLKEAWKDLVKAYLQEAKWRH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   616 DKSTPSLEDYMENAYISFALGPIVLPATYLIGPPLPEKTVDS-HQYNQLYKLVSTMGRLLNDIQGFKRESAEGKL-NAVS 693
Cdd:pfam03936 160 EGYVPTFEEYLENGVVSSGYPLLLLHSFVGMGDLITKEAFEWlKSYPKIVRASSTIGRLLNDIATYEDEQERGGVaSSVE 239
                         250       260
                  ....*....|....*....|....*....
gi 15219383   694 LHMKHErdNRSKEVIIESMKGLAERKREE 722
Cdd:pfam03936 240 CYMKEH--GVSEEEAREEIRKLIEDAWKD 266
 
Name Accession Description Interval E-value
PLN02279 PLN02279
ent-kaur-16-ene synthase
1-785 0e+00

ent-kaur-16-ene synthase


Pssm-ID: 177918 [Multi-domain]  Cd Length: 784  Bit Score: 1420.81  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383    1 MSINLRSSGCSSPISATLERRLDSEVQTRANNVSFEQTKEKIRKMLEKVELSVSAYDTSWVAMVPSPSSQNAPLFPQCVK 80
Cdd:PLN02279   1 MSINLRSSGCSSPISATLEPRLKTWTQTRANNVSFEGTKERIKKMFDKVELSVSSYDTAWVAMVPSPNSQQAPLFPECVK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   81 WLLDNQHEDGSWGLDnHDHQSLKKDVLSSTLASILALKKWGIGERQINKGLQFIELNSALVTDETIQKPTGFDIIFPGMI 160
Cdd:PLN02279  81 WLLENQLEDGSWGLP-HDHPLLVKDALSSTLASILALKKWGVGEEQINKGLQFIELNSASVTDEKQHKPIGFDIIFPGMI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  161 KYARDLNLTIPLGSEVVDDMIRKRDLDLKCDSEKFSKGREAYLAYVLEGTRNLKDWDLIVKYQRKNGSLFDSPATTAAAF 240
Cdd:PLN02279 160 EYAKDLDLNLPLGSEVVDAMLHKRDLDLKSGGGSNTKGREAYLAYVSEGIGKLQDWEMVMKYQRKNGSLFNSPSTTAAAF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  241 TQFGNDGCLRYLCSLLQKFEAAVPSVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCA 320
Cdd:PLN02279 240 SHLQNAGCLRYLRSLLQKFGNAVPTVYPLDQYARLSMVDTLERLGIDRHFRKEIKSVLDETYRYWLQGEEEIFLDLATCA 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  321 LAFRLLLAHGYDVSYDPLKPFAEESgFSDTLEGYVKNTFSVLELFKAAQ-SYPHESALKKQCCWTKQYLEMELSSWVKTS 399
Cdd:PLN02279 320 LAFRILRLNGYDVSSDPLKQFAEDH-FSDSLGGYLKDTGAVLELFRASQiSYPDESLLEKQNSWTSHFLEQGLSNWSKTA 398
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  400 VR-DKYLKKEVEDALAFPSYASLERSDHRRKILNgSAVENTRVTKTSYRLHNICTSDILKLAVDDFNFCQSIHREEMERL 478
Cdd:PLN02279 399 DRlRKYIKKEVEDALNFPYYANLERLANRRSIEN-YAVDDTRILKTSYRCSNICNQDFLKLAVEDFNFCQSIHREELKQL 477
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  479 DRWIVENRLQELKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLNGV 558
Cdd:PLN02279 478 ERWIVENRLDKLKFARQKLAYCYFSAAATLFSPELSDARLSWAKNGVLTTVVDDFFDVGGSEEELENLIQLVEKWDVNGS 557
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  559 PEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPI 638
Cdd:PLN02279 558 PDFCSEQVEIIFSALRSTISEIGDKAFTWQGRNVTSHIIKIWLDLLKSMLTEAQWSSNKSTPTLDEYMTNAYVSFALGPI 637
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  639 VLPATYLIGPPLPEKTVDSHQYNQLYKLVSTMGRLLNDIQGFKRESAEGKLNAVSLHMKHERDNRSKEVIIESMKGLAER 718
Cdd:PLN02279 638 VLPALYLVGPKLSEEVVDSPELHKLYKLMSTCGRLLNDIRGFKRESKEGKLNAVSLHMIHGNGNSTEEEAIESMKGLIES 717
                        730       740       750       760       770       780
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15219383  719 KREELHKLVLEEKGSVVPRECKEAFLKMSKVLNLFYRKDDGFTSNDLMSLVKSVIYEPVSLQEESLT 785
Cdd:PLN02279 718 QRRELLRLVLQEKGSNVPRECKDLFWKMSKVLHLFYRKDDGFTSNDMMSLVKSVIYEPVSLQEESLT 784
Terpene_cyclase_plant_C1 cd00684
Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene ...
265-776 4.07e-178

Plant Terpene Cyclases, Class 1; This CD includes a diverse group of monomeric plant terpene cyclases (Tspa-Tspf) that convert the acyclic isoprenoid diphosphates, geranyl diphosphate (GPP), farnesyl diphosphate (FPP), or geranylgeranyl diphosphate (GGPP) into cyclic monoterpenes, diterpenes, or sesquiterpenes, respectively; a few form acyclic species. Terpnoid cyclases are soluble enzymes localized to the cytosol (sesquiterpene synthases) or plastids (mono- and diterpene synthases). All monoterpene and diterpene synthases have restrict substrate specificity, however, some sesquiterpene synthases can accept both FPP and GPP. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl diphosphates, via bridging Mg2+ ions (K+ preferred by gymnosperm cyclases), inducing conformational changes such that an N-terminal region forms a cap over the catalytic core. Loss of diphosphate from the enzyme-bound substrate (GPP, FPP, or GGPP) results in an allylic carbocation that electrophilically attacks a double bond further down the terpene chain to effect the first ring closure. Unlike monoterpene, sesquiterene, and macrocyclic diterpenes synthases, which undergo substrate ionization by diphosphate ester scission, Tpsc-like diterpene synthases catalyze cyclization reactions by an initial protonation step producing a copalyl diphosphate intermediate. These enzymes lack the aspartate-rich sequences mentioned above. Most diterpene synthases have an N-terminal, internal element (approx 210 aa) whose function is unknown.


Pssm-ID: 173832 [Multi-domain]  Cd Length: 542  Bit Score: 521.76  E-value: 4.07e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 265 SVYPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWLRGDEEICLDLATCALAFRLLLAHGYDVSYDPLKPFAEE 344
Cdd:cd00684  47 SEYPVDLFERLWLIDRLQRLGISYHFEDEIKEILDYIYRYWTERGESNEDDLYTTALGFRLLRQHGYNVSSDVFKKFKDE 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 345 SG-FSDTLegyVKNTFSVLELFKAAQ-SYPHESALKKQCCWTKQYLEMELSSWvktSVRDKYLKKEVEDALAFPSYASLE 422
Cdd:cd00684 127 DGkFKESL---TQDVKGMLSLYEASHlSFPGEDILDEALSFTTKHLEEKLESN---WIIDPDLSGEIEYALEIPLHASLP 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 423 RSDHRRKILNGSAVENtrvtktsyrlHNictSDILKLAVDDFNFCQSIHREEMERLDRWIVENRLQE-LKFARQKLAYCY 501
Cdd:cd00684 201 RLEARWYIEFYEQEDD----------HN---ETLLELAKLDFNILQALHQEELKILSRWWKDLDLASkLPFARDRLVECY 267
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 502 FSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLNGVpEYSSEHVEIIFSVLRDTILETG 581
Cdd:cd00684 268 FWAAGTYFEPQYSLARIALAKTIALITVIDDTYDVYGTLEELELFTEAVERWDISAI-DQLPEYMKIVFKALLNTVNEIE 346
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 582 DKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPIVLPATYLIGPPLPEKTVDSHQYN 661
Cdd:cd00684 347 EELLKEGGSYVVPYLKEAWKDLVKAYLVEAKWAHEGYVPTFEEYMENALVSIGLGPLLLTSFLGMGDILTEEAFEWLESR 426
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 662 Q-LYKLVSTMGRLLNDIQGFKRESAEGK-LNAVSLHMKHErdNRSKEVIIESMKGLAERKREELHKLVLEEKgSVVPREC 739
Cdd:cd00684 427 PkLVRASSTIGRLMNDIATYEDEMKRGDvASSIECYMKEY--GVSEEEAREEIKKMIEDAWKELNEEFLKPS-SDVPRPI 503
                       490       500       510
                ....*....|....*....|....*....|....*....
gi 15219383 740 KEAFLKMSKVLNLFYRKDDGFTSND--LMSLVKSVIYEP 776
Cdd:cd00684 504 KQRFLNLARVIDVFYKEGDGFTHPEgeIKDHITSLLFEP 542
PLN02592 PLN02592
ent-copalyl diphosphate synthase
31-748 1.71e-105

ent-copalyl diphosphate synthase


Pssm-ID: 215321 [Multi-domain]  Cd Length: 800  Bit Score: 341.85  E-value: 1.71e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   31 NNVSFEQTKEKIRKMLEKV---ELSVSAYDTSWVAMVPSPSSQNAPLFPQCVKWLLDNQHEDGSWGldnHDHQSLKKDVL 107
Cdd:PLN02592  70 VSNEIKERVKTVKSMLSSMedgEISISAYDTAWVALVEDINGSGTPQFPSSLQWIANNQLSDGSWG---DAYLFSAHDRL 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  108 SSTLASILALKKWGIGERQINKGLQFIELNSALVTDETIQK-PTGFDIIFPGMIKYARDLNLTIPLGSEVVDDMIRKRDL 186
Cdd:PLN02592 147 INTLACVVALKSWNLHPEKCEKGMSFFRENICKLEDENAEHmPIGFEVAFPSLLEIAKNLDIEVPYDSPVLKEIYAQRNL 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  187 DLKCDSEKFSKGREAYLAYVLEGTRNLkDWDLIVKYQRKNGSLFDSPATTAAAFTQFGNDGCLRYLCSLLQKFEAAVPSV 266
Cdd:PLN02592 227 KLTRIPKDIMHKVPTTLLHSLEGMPGL-DWEKLLKLQCQDGSFLFSPSSTAFALMQTKDENCLEYLNKAVQRFNGGVPNV 305
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  267 YPFDQYARLSIIVTLESLGIDRDFKTEIKSILDETYRYWlrGDEEICL-------DLATCALAFRLLLAHGYDVSYDPLK 339
Cdd:PLN02592 306 YPVDLFEHIWAVDRLQRLGISRYFEPEIKECIDYVHRYW--TENGICWarnshvhDIDDTAMGFRLLRLHGHQVSADVFK 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  340 PFAEESGFSDTLEGYVKNTFSVLELFKAAQ-SYPHESALKKQCCWTKQYLEME------LSSWVKTsvrdKYLKKEVEDA 412
Cdd:PLN02592 384 HFEKGGEFFCFAGQSTQAVTGMFNLYRASQvLFPGEKILENAKEFSSKFLREKqeanelLDKWIIM----KDLPGEVGFA 459
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  413 LAFPSYASLERSDHRRKILNGSAVENTRVTKTSYRLHNICTSDILKLAVDDFNFCQSIHREEMERLDRWIVENRLQELKF 492
Cdd:PLN02592 460 LEIPWYASLPRVETRFYIEQYGGEDDVWIGKTLYRMPYVNNNEYLELAKLDYNNCQALHQLEWDNFQKWYEECNLGEFGV 539
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  493 ARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIH-LVEKWDLNGvpeYSSEHVEIIFS 571
Cdd:PLN02592 540 SRSELLLAYFLAAASIFEPERSHERLAWAKTTVLVEAISSYFNKETSSKQRRAFLHeFGYGYKING---RRSDHHFNDRN 616
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  572 VLRDTILETGDK---------------AFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKStpsledymenayiSFALG 636
Cdd:PLN02592 617 MRRSGSVKTGEElvglllgtlnqlsldALEAHGRDISHLLRHAWEMWLLKWLLEGDGRQGEA-------------ELLVK 683
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383  637 PIVLPATYLIgpplPEKTVDSHQYNQLYKLVStmgRLLNDIQGFKRESAEGKlnavslhmkhERDNRSKEVIIESMkgla 716
Cdd:PLN02592 684 TINLTAGRSL----SEELLAHPQYEQLAQLTN---RICYQLGHYKKNKVHIN----------TYNPEEKSKTTPSI---- 742
                        730       740       750
                 ....*....|....*....|....*....|..
gi 15219383  717 ERKREELHKLVLEEKGSVVPRECKEAFLKMSK 748
Cdd:PLN02592 743 ESDMQELVQLVLQNSSDDIDPVIKQTFLMVAK 774
Terpene_synth_C pfam03936
Terpene synthase family, metal binding domain; It has been suggested that this gene family be ...
457-722 1.64e-94

Terpene synthase family, metal binding domain; It has been suggested that this gene family be designated tps (for terpene synthase). It has been split into six subgroups on the basis of phylogeny, called tpsa-tpsf. tpsa includes vetispiridiene synthase, 5-epi- aristolochene synthase, and (+)-delta-cadinene synthase. tpsb includes (-)-limonene synthase. tpsc includes kaurene synthase A. tpsd includes taxadiene synthase, pinene synthase, and myrcene synthase. tpse includes kaurene synthase B. tpsf includes linalool synthase.


Pssm-ID: 461096 [Multi-domain]  Cd Length: 266  Bit Score: 295.59  E-value: 1.64e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   457 LKLAVDDFNFCQSIHREEMERLDRWIVENRLQE-LKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFD 535
Cdd:pfam03936   1 LELAKLDFNLLQSLHQKELKELTRWWKELGLASkLPFARDRLVECYFWALGVYFEPQYSRARIILAKVIVLITIIDDTYD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   536 VGGSKEELENLIHLVEKWDLNGVpEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSS 615
Cdd:pfam03936  81 VYGTLEELELLTEAVERWDESAI-EQLPEYMKICFKALLNTFNEIEEELSKGKGYNVIPYLKEAWKDLVKAYLQEAKWRH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   616 DKSTPSLEDYMENAYISFALGPIVLPATYLIGPPLPEKTVDS-HQYNQLYKLVSTMGRLLNDIQGFKRESAEGKL-NAVS 693
Cdd:pfam03936 160 EGYVPTFEEYLENGVVSSGYPLLLLHSFVGMGDLITKEAFEWlKSYPKIVRASSTIGRLLNDIATYEDEQERGGVaSSVE 239
                         250       260
                  ....*....|....*....|....*....
gi 15219383   694 LHMKHErdNRSKEVIIESMKGLAERKREE 722
Cdd:pfam03936 240 CYMKEH--GVSEEEAREEIRKLIEDAWKD 266
Terpene_cyclase_C1 cd00868
Terpene cyclases, Class 1; Terpene cyclases, Class 1 (C1) of the class 1 family of isoprenoid ...
470-754 5.65e-80

Terpene cyclases, Class 1; Terpene cyclases, Class 1 (C1) of the class 1 family of isoprenoid biosynthesis enzymes, which share the 'isoprenoid synthase fold' and convert linear, all-trans, isoprenoids, geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate into numerous cyclic forms of monoterpenes, diterpenes, and sesquiterpenes. Also included in this CD are the cis-trans terpene cyclases such as trichodiene synthase. The class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD. Taxonomic distribution includes bacteria, fungi and plants.


Pssm-ID: 173837 [Multi-domain]  Cd Length: 284  Bit Score: 258.06  E-value: 5.65e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 470 IHREEMERLDRWIVENRLQE-LKFARQKLAYCYFSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIH 548
Cdd:cd00868   1 LHQEELKELSRWWKELGLQEkLPFARDRLVECYFWAAGSYFEPQYSEARIALAKTIALLTVIDDTYDDYGTLEELELFTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 549 LVEKWDLNgVPEYSSEHVEIIFSVLRDTILETGDKAFTYQGRNVTHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMEN 628
Cdd:cd00868  81 AVERWDIS-AIDELPEYMKPVFKALYDLVNEIEEELAKEGGSESLPYLKEAWKDLLRAYLVEAKWANEGYVPSFEEYLEN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 629 AYISFALGPIVLPATYLIGPPLPEKTVD-SHQYNQLYKLVSTMGRLLNDIQGFKRESAEGKL-NAVSLHMKHerDNRSKE 706
Cdd:cd00868 160 RRVSIGYPPLLALSFLGMGDILPEEAFEwLPSYPKLVRASSTIGRLLNDIASYEKEIARGEVaNSVECYMKE--YGVSEE 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15219383 707 VIIESMKGLAERKREELHKLVLEEKgSVVPRECKEAFLKMSKVLNLFY 754
Cdd:cd00868 238 EALEELRKMIEEAWKELNEEVLKLS-SDVPRAVLETLLNLARGIYVWY 284
Terpene_synth pfam01397
Terpene synthase, N-terminal domain; It has been suggested that this gene family be designated ...
215-413 7.35e-43

Terpene synthase, N-terminal domain; It has been suggested that this gene family be designated tps (for terpene synthase). It has been split into six subgroups on the basis of phylogeny, called tpsa-tpsf. tpsa includes vetispiridiene synthase, 5-epi- aristolochene synthase, and (+)-delta-cadinene synthase. tpsb includes (-)-limonene synthase. tpsc includes kaurene synthase A. tpsd includes taxadiene synthase, pinene synthase and myrcene synthase. tpse includes kaurene synthase B. tpsf includes linalool synthase.


Pssm-ID: 460194 [Multi-domain]  Cd Length: 190  Bit Score: 153.90  E-value: 7.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   215 DWDLIVKYQRKNGSLFDSPatTAAAFTqfgndgclRYLCSLLQKFE---AAVPSVYPFDQYARLSIIVTLESLGIDRDFK 291
Cdd:pfam01397   1 DWGDHFLLSLSNGSLFNSP--TAEALM--------REAEDLKEEVRkmlKAVPTVYPVDLKEKLELIDTLQRLGISYHFE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   292 TEIKSILDETYRYWLR-GDEEICLDLATCALAFRLLLAHGYDVSYDPLKPFAEESG-FSDTLEGYVKntfSVLELFKAAQ 369
Cdd:pfam01397  71 KEIEEILDQIYRNWEDdGIEDDDLDLYTTALAFRLLRQHGYDVSSDVFNKFKDEDGnFKECLSEDVK---GLLSLYEASH 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 15219383   370 -SYPHESALKKQCCWTKQYLEMELSSWVKTSVRDkyLKKEVEDAL 413
Cdd:pfam01397 148 lSTPGEDILDEALSFTRSHLKESLAGNLGLISPH--LAEEVEHAL 190
Terpene_syn_C_2 pfam19086
Terpene synthase family 2, C-terminal metal binding;
525-722 3.60e-41

Terpene synthase family 2, C-terminal metal binding;


Pssm-ID: 465972 [Multi-domain]  Cd Length: 199  Bit Score: 149.29  E-value: 3.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   525 VLTTVVDDFFDVG-GSKEELENLIHLVEKWD--LNGVPEYSSEHVEIIFSVLRDTILETGDKAftyqGRNVTHHIVKIWL 601
Cdd:pfam19086   4 AWLFILDDIYDEVyGTLEELELFTEAIERWDalLPLDGPELPEYMKPLYRALADLWERLAKEA----SPDWRRRFKEAWK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383   602 DLLKSMLREAEWSSDKSTPSLEDYMENAYISFALGPIVLPATYLIGPPLPEKTVDSHQYNQLYKLVSTMGRLLNDIQGFK 681
Cdd:pfam19086  80 DYLDAYLWEAKWRASGYVPTLEEYLELRRVTSGVPPLLALIEFGLGIELPDEVFEHPVVRRLVRAASDIVRLVNDLFSYK 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 15219383   682 RESAEGKL-NAVSLHMKHErdNRSKEVIIESMKGLAERKREE 722
Cdd:pfam19086 160 KEQARGDVhNLVLVLMKEY--GVSLQEAVDEVGELIEEAWKD 199
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
502-748 5.10e-29

Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases (IPPS) and class I terpene cyclases which either synthesis geranyl/farnesyl diphosphates (GPP/FPP) or longer chained products from isoprene precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), or use geranyl (C10)-, farnesyl (C15)-, or geranylgeranyl (C20)-diphosphate as substrate. These enzymes produce a myriad of precursors for such end products as steroids, cholesterol, sesquiterpenes, heme, carotenoids, retinoids, and diterpenes; and are widely distributed among archaea, bacteria, and eukaryota.The enzymes in this superfamily share the same 'isoprenoid synthase fold' and include several subgroups. The head-to-tail (HT) IPPS catalyze the successive 1'-4 condensation of the 5-carbon IPP to the growing isoprene chain to form linear, all-trans, C10-, C15-, C20- C25-, C30-, C35-, C40-, C45-, or C50-isoprenoid diphosphates. Cyclic monoterpenes, diterpenes, and sesquiterpenes, are formed from their respective linear isoprenoid diphosphates by class I terpene cyclases. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Cyclization of these 30- and 40-carbon linear forms are catalyzed by class II cyclases. Both the isoprenoid chain elongation reactions and the class I terpene cyclization reactions proceed via electrophilic alkylations in which a new carbon-carbon single bond is generated through interaction between a highly reactive electron-deficient allylic carbocation and an electron-rich carbon-carbon double bond. The catalytic site consists of a large central cavity formed by mostly antiparallel alpha helices with two aspartate-rich regions located on opposite walls. These residues mediate binding of prenyl phosphates via bridging Mg2+ ions, inducing proposed conformational changes that close the active site to solvent, stabilizing reactive carbocation intermediates. Generally, the enzymes in this family exhibit an all-trans reaction pathway, an exception, is the cis-trans terpene cyclase, trichodiene synthase. Mechanistically and structurally distinct, class II terpene cyclases and cis-IPPS are not included in this CD.


Pssm-ID: 173830 [Multi-domain]  Cd Length: 243  Bit Score: 116.06  E-value: 5.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 502 FSGAATLFSPELSDARISWAKGGVLTTVVDDFFDVGGSKEELENLIHLVEKWDLngvpeysSEHVEIIFSVLRDTILETG 581
Cdd:cd00385   1 FRPLAVLLEPEASRLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAVAIDGL-------PEAILAGDLLLADAFEELA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 582 DKAftyqGRNVTHHIVKIWLDLLKSMLREAEWSSDKStPSLEDYMENAYISFAlGPIVLPATYLIGPPLPEKTVDsHQYN 661
Cdd:cd00385  74 REG----SPEALEILAEALLDLLEGQLLDLKWRREYV-PTLEEYLEYCRYKTA-GLVGALCLLGAGLSGGEAELL-EALR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 662 QLYKLVSTMGRLLNDIQGFKRESA--EGKLNAVSLHMKHE----------RDNRSKEVIIESMKGLAERKREELHKLVLE 729
Cdd:cd00385 147 KLGRALGLAFQLTNDLLDYEGDAErgEGKCTLPVLYALEYgvpaedlllvEKSGSLEEALEELAKLAEEALKELNELILS 226
                       250
                ....*....|....*....
gi 15219383 730 EKGsvVPRECKEAFLKMSK 748
Cdd:cd00385 227 LPD--VPRALLALALNLYR 243
Terpene_cyclase_nonplant_C1 cd00687
Non-plant Terpene Cyclases, Class 1; This CD includes terpenoid cyclases such as pentalenene ...
476-745 3.59e-10

Non-plant Terpene Cyclases, Class 1; This CD includes terpenoid cyclases such as pentalenene synthase and aristolochene synthase which, using an all-trans pathway, catalyze the ionization of farnesyl diphosphate, followed by the formation of a macrocyclic intermediate by bond formation between C1 with either C10 (aristolochene synthase) or C11 (pentalenene synthase), resulting in production of tricyclic hydrocarbon pentalenene or bicyclic hydrocarbon aristolochene. As with other enzymes with the 'terpenoid synthase fold', they have two conserved metal binding motifs, proposed to coordinate Mg2+ ion-bridged binding of the diphosphate moiety of FPP to the enzymes. Metal-triggered substrate ionization initiates catalysis, and the alpha-barrel active site serves as a template to channel and stabilize the conformations of reactive carbocation intermediates through a complex cyclization cascade. These enzymes function in the monomeric form and are found in fungi, bacteria and Dictyostelium.


Pssm-ID: 173835 [Multi-domain]  Cd Length: 303  Bit Score: 62.00  E-value: 3.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 476 ERLDRWIVENRLQELKFARQKLAYCYFSGAATLFSPELSDARISWAkGGVLT--TVVDDFFDVGGSK-EELENLI-HLVE 551
Cdd:cd00687  17 DEYLEWVLEEMLIPSEKAEKRFLSADFGDLAALFYPDADDERLMLA-ADLMAwlFVFDDLLDRDQKSpEDGEAGVtRLLD 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 552 KWDLNGVPEYS-SEHVEIIFSVLRDTILETGDKAFTyqgrnvtHHIVKIWLDLLKSMLREAEWSSDKSTPSLEDYMENAY 630
Cdd:cd00687  96 ILRGDGLDSPDdATPLEFGLADLWRRTLARMSAEWF-------NRFAHYTEDYFDAYIWEGKNRLNGHVPDVAEYLEMRR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15219383 631 ISFALGPIVLPATYLIGPPLPEKTVDSHQYNQLYKLVSTMGRLLNDIQGFKRE-SAEGK-LNAVSLHMKHErdNRSKEvi 708
Cdd:cd00687 169 FNIGADPCLGLSEFIGGPEVPAAVRLDPVMRALEALASDAIALVNDIYSYEKEiKANGEvHNLVKVLAEEH--GLSLE-- 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15219383 709 iESMKGLAERKREELH---KLVLEEKGSVVPRECKEAFLK 745
Cdd:cd00687 245 -EAISVVRDMHNERITqfeELEASLIKSGDLEEESPAVRA 283
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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