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Conserved domains on  [gi|1063946782|gb|ODS59644|]
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hypothetical protein ABS36_00740 [Acidobacteria bacterium SCN 69-37]

Protein Classification

polyprenyl synthetase family protein( domain architecture ID 10000639)

polyprenyl synthetase family protein such as farnesyl/geranylgeranyl diphosphate synthase, which is a key enzyme in isoprenoid biosynthesis, catalyzing the formation of farnesyl diphosphate (FPP) and geranylgeranyl diphosphate (GGPP), respectively

CATH:  1.10.600.10
EC:  2.5.1.-
Gene Ontology:  GO:0004659|GO:0046872|GO:0008299
SCOP:  4001453

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-320 1.00e-123

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


:

Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 357.61  E-value: 1.00e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   1 MFEPVRAELARVEREFAKHLE-SRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHD 79
Cdd:COG0142     6 LLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASLVHD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  80 DIIDSAETRRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGN----IEVVRLLCDCTLRLIEGELYQLTKTGDAAITE 155
Cdd:COG0142    86 DVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRLDVTL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 156 AEHFEIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPI 235
Cdd:COG0142   166 EEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 236 ILMLQRAGAEGEQAVLPVIADGQVTPEQWRTIRDLLERHGAIDAAFERAVRHADRAKQHlLEAFPASAERDSLVALADYV 315
Cdd:COG0142   246 LLALERADPEERAELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAA-LAALPDSEAREALRALADYV 324

                  ....*
gi 1063946782 316 IHRDR 320
Cdd:COG0142   325 VERDR 329
 
Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-320 1.00e-123

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 357.61  E-value: 1.00e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   1 MFEPVRAELARVEREFAKHLE-SRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHD 79
Cdd:COG0142     6 LLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASLVHD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  80 DIIDSAETRRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGN----IEVVRLLCDCTLRLIEGELYQLTKTGDAAITE 155
Cdd:COG0142    86 DVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRLDVTL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 156 AEHFEIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPI 235
Cdd:COG0142   166 EEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 236 ILMLQRAGAEGEQAVLPVIADGQVTPEQWRTIRDLLERHGAIDAAFERAVRHADRAKQHlLEAFPASAERDSLVALADYV 315
Cdd:COG0142   246 LLALERADPEERAELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAA-LAALPDSEAREALRALADYV 324

                  ....*
gi 1063946782 316 IHRDR 320
Cdd:COG0142   325 VERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
22-318 8.30e-88

Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation 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 (DDXX(XX)D) 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, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.


Pssm-ID: 173833  Cd Length: 259  Bit Score: 263.64  E-value: 8.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  22 SRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLN-AAVVEFVHTATLVHDDIIDSAETRRGRLTAHSRWGS 100
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPELEAALRlAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 101 DITVLLGDYLYIRSMAMALSQGN---IEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTAYLFAGCAEIG 177
Cdd:cd00685    81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 178 GMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILmlqragaegeqavlpviadg 257
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLL-------------------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063946782 258 qvtpeqwrtirdllerhgaidAAFERAVRHADRAKQHlLEAFPASAERDSLVALADYVIHR 318
Cdd:cd00685   221 ---------------------ALRELAREYEEKALEA-LKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
24-286 5.63e-84

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 253.58  E-value: 5.63e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  24 VELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLN--AAVVEFVHTATLVHDDIIDSAETRRGRLTAHSRWGSD 101
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEKAIvlAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 102 ITVLLGDYLYIRSMAMALS-QGNIEVVRLLCDCTLRLIEGELYQLT--KTGDAAITEAEHFEIIRHKTAYLFAGCAEIGG 178
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKlFPNPELLELFSEVTLQTAEGQGLDLLwrNDDDLSCTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 179 MLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQRagaegeqavlpviadgq 258
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER----------------- 223
                         250       260
                  ....*....|....*....|....*...
gi 1063946782 259 vTPEQWRTIRDLLERHGAIDAAFERAVR 286
Cdd:pfam00348 224 -TPEQRKILLEIYGKRPEDVEKVKEAYE 250
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
8-320 2.94e-74

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 231.27  E-value: 2.94e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   8 ELARVEREFAKHLESRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHDDIIDSAET 87
Cdd:PRK10888   13 DMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  88 RRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTA 167
Cdd:PRK10888   93 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 168 YLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQRAgaege 247
Cdd:PRK10888  173 RLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHG----- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 248 qavlpviadgqvTPEQWRTIRDLLE----RH------------GAIDAAFERAVRHADRAKQhLLEAFPASAERDSLVAL 311
Cdd:PRK10888  248 ------------TPEQAAMIRTAIEqgngRHllepvleamnacGSLEWTRQRAEEEADKAIA-ALQVLPDTPWREALIGL 314

                  ....*....
gi 1063946782 312 ADYVIHRDR 320
Cdd:PRK10888  315 AHIAVQRDR 323
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
1-319 3.18e-57

heptaprenyl diphosphate synthase component II; Members of this family are component II of the heterodimeric heptaprenyl diphosphate synthase. The trusted cutoff was set such that all members identified are encoded near to a recognizable gene for component I (in pfam07307). This enzyme acts in menaquinone-7 isoprenoid side chain biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131795  Cd Length: 319  Bit Score: 187.23  E-value: 3.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   1 MFEPVRAELARVEREFAKHLESRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDlAVLNAAV-VEFVHTATLVHD 79
Cdd:TIGR02748   5 IYSFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLD-AIKHVAVaLELIHMASLVHD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  80 DIIDSAETRRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHF 159
Cdd:TIGR02748  84 DVIDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 160 EIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILML 239
Cdd:TIGR02748 164 RRIKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAM 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 240 QRAGAegEQAVLPVIADgqVTPEQWRTIRDLLERHGAIDAAFERAVRHADRAkQHLLEAFPASAERDSLVALADYVIHRD 319
Cdd:TIGR02748 244 EDPFL--KKRIEQVLEE--TTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKA-LELLDGLPDGRAKKPLQEIAKYIGKRK 318
hexpp_archaea NF040936
hexaprenyl pyrophosphate synthase;
29-211 1.82e-12

hexaprenyl pyrophosphate synthase;


Pssm-ID: 468868  Cd Length: 275  Bit Score: 66.24  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  29 EMGRYVqMSGGKRVRpAVLLM--AARLCG-----YTGDLAVlnaavvEFVHTATLVHDDIIDSAETRRGRLTAHSRWGSD 101
Cdd:NF040936   32 EMSKYI-MKDGKRFR-GTLMFlfTEALGGeekdaYKGALAT------EILHSASLALDDIVDYDLTRRGDKSAWAVYTNR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 102 ITVLLGDYLYIRSMAMALSQGnievvrllcDCTLRlIEGELYQLTKTG---DAAITEAEHFEIIRHKTAYLFagcaEIGG 178
Cdd:NF040936  104 RVIFVSNYLIPTALNIISSYG---------EDALK-ISIELWKDTAVGalkDMYGNKEDYFKTIELKTASLF----KLST 169
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063946782 179 MLGdADSARRTA----LREYGFDLGIAFQIVDDVLDY 211
Cdd:NF040936  170 MLA-SFSSRREElldeLLDAGKYLGIIYQLIDDYVDC 205
 
Name Accession Description Interval E-value
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
1-320 1.00e-123

Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl pyrophosphate synthase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 439912 [Multi-domain]  Cd Length: 329  Bit Score: 357.61  E-value: 1.00e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   1 MFEPVRAELARVEREFAKHLE-SRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHD 79
Cdd:COG0142     6 LLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTASLVHD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  80 DIIDSAETRRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGN----IEVVRLLCDCTLRLIEGELYQLTKTGDAAITE 155
Cdd:COG0142    86 DVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGRLDVTL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 156 AEHFEIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPI 235
Cdd:COG0142   166 EEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGKPTLPL 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 236 ILMLQRAGAEGEQAVLPVIADGQVTPEQWRTIRDLLERHGAIDAAFERAVRHADRAKQHlLEAFPASAERDSLVALADYV 315
Cdd:COG0142   246 LLALERADPEERAELRELLGKPDLDEEDLAEVRALLRESGALEYARELARELAEEALAA-LAALPDSEAREALRALADYV 324

                  ....*
gi 1063946782 316 IHRDR 320
Cdd:COG0142   325 VERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
22-318 8.30e-88

Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) catalyze head-to-tail (HT) (1'-4) condensation reactions. This CD includes all-trans (E)-isoprenyl diphosphate synthases which synthesize various chain length (C10, C15, C20, C25, C30, C35, C40, C45, and C50) linear isoprenyl diphosphates from precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). They catalyze the successive 1'-4 condensation of the 5-carbon IPP to allylic substrates geranyl-, farnesyl-, or geranylgeranyl-diphosphate. Isoprenoid chain elongation 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 (DDXX(XX)D) 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, protecting and stabilizing reactive carbocation intermediates. Farnesyl diphosphate synthases produce the precursors of steroids, cholesterol, sesquiterpenes, farnsylated proteins, heme, and vitamin K12; and geranylgeranyl diphosphate and longer chain synthases produce the precursors of carotenoids, retinoids, diterpenes, geranylgeranylated chlorophylls, ubiquinone, and archaeal ether linked lipids. Isoprenyl diphosphate synthases are widely distributed among archaea, bacteria, and eukareya.


Pssm-ID: 173833  Cd Length: 259  Bit Score: 263.64  E-value: 8.30e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  22 SRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLN-AAVVEFVHTATLVHDDIIDSAETRRGRLTAHSRWGS 100
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPELEAALRlAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 101 DITVLLGDYLYIRSMAMALSQGN---IEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTAYLFAGCAEIG 177
Cdd:cd00685    81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 178 GMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILmlqragaegeqavlpviadg 257
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLL-------------------- 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063946782 258 qvtpeqwrtirdllerhgaidAAFERAVRHADRAKQHlLEAFPASAERDSLVALADYVIHR 318
Cdd:cd00685   221 ---------------------ALRELAREYEEKALEA-LKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
24-286 5.63e-84

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 253.58  E-value: 5.63e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  24 VELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLN--AAVVEFVHTATLVHDDIIDSAETRRGRLTAHSRWGSD 101
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGGPEDLEKAIvlAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 102 ITVLLGDYLYIRSMAMALS-QGNIEVVRLLCDCTLRLIEGELYQLT--KTGDAAITEAEHFEIIRHKTAYLFAGCAEIGG 178
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKlFPNPELLELFSEVTLQTAEGQGLDLLwrNDDDLSCTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 179 MLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQRagaegeqavlpviadgq 258
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER----------------- 223
                         250       260
                  ....*....|....*....|....*...
gi 1063946782 259 vTPEQWRTIRDLLERHGAIDAAFERAVR 286
Cdd:pfam00348 224 -TPEQRKILLEIYGKRPEDVEKVKEAYE 250
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
8-320 2.94e-74

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 231.27  E-value: 2.94e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   8 ELARVEREFAKHLESRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHDDIIDSAET 87
Cdd:PRK10888   13 DMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDM 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  88 RRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTA 167
Cdd:PRK10888   93 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 168 YLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQRAgaege 247
Cdd:PRK10888  173 RLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPLLHAMHHG----- 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 248 qavlpviadgqvTPEQWRTIRDLLE----RH------------GAIDAAFERAVRHADRAKQhLLEAFPASAERDSLVAL 311
Cdd:PRK10888  248 ------------TPEQAAMIRTAIEqgngRHllepvleamnacGSLEWTRQRAEEEADKAIA-ALQVLPDTPWREALIGL 314

                  ....*....
gi 1063946782 312 ADYVIHRDR 320
Cdd:PRK10888  315 AHIAVQRDR 323
preA CHL00151
prenyl transferase; Reviewed
1-320 1.76e-64

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 206.18  E-value: 1.76e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   1 MFEPVRAELARVEREFAKHLESRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLN---AAVVEFVHTATLV 77
Cdd:CHL00151    7 LLTPIEEELLILEDNLKKLIGSGHPILYAAAKHLFSAGGKRIRPAIVLLVAKATGGNMEIKTSQqrlAEITEIIHTASLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  78 HDDIIDSAETRRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAE 157
Cdd:CHL00151   87 HDDVIDECSIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 158 HFEIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIIL 237
Cdd:CHL00151  167 YIEKSFYKTASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLF 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 238 MLQRagaEGEQAvlPVIADGQVTPEQWRTIRDLLERHGAIDAAFERAVRHADRAKQhLLEAFPASAERDSLVALADYVIH 317
Cdd:CHL00151  247 ALTQ---NSKLA--KLIEREFCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQ-CLKFLPPSSAKDSLIEIANFIIN 320

                  ...
gi 1063946782 318 RDR 320
Cdd:CHL00151  321 RLN 323
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
42-283 1.38e-60

Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of class 1 isoprenoid biosynthesis enzymes 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, diterpenes, ubiquinone, and archaeal ether linked lipids; and are widely distributed among archaea, bacteria, and eukareya. The enzymes in this family share the same 'isoprenoid synthase fold' and include the head-to-tail (HT) IPPS which 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. The head-to-head (HH) IPPS catalyze the successive 1'-1 condensation of 2 farnesyl or 2 geranylgeranyl isoprenoid diphosphates. Isoprenoid chain elongation 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, cis-IPPS are not included in this CD.


Pssm-ID: 173836  Cd Length: 236  Bit Score: 193.33  E-value: 1.38e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  42 VRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHDDIIDSAETRRGRLTAHSR-WGSDITVLLGDYLYIRSMAMALS 120
Cdd:cd00867     1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLRrFGNALAILAGDYLLARAFQLLAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 121 QGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGI 200
Cdd:cd00867    81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 201 AFQIVDDVLDYTADETTLGKPlGGDLREGKVTLPIILMLQRAGAEGEQAvlpvIADGQVTPEQWRTIRDLLERhgAIDAA 280
Cdd:cd00867   161 AFQLTDDLLDVFGDAEELGKV-GSDLREGRITLPVILARERAAEYAEEA----YAALEALPPSLPRARRALIA--LADFL 233

                  ...
gi 1063946782 281 FER 283
Cdd:cd00867   234 YRR 236
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
1-319 3.18e-57

heptaprenyl diphosphate synthase component II; Members of this family are component II of the heterodimeric heptaprenyl diphosphate synthase. The trusted cutoff was set such that all members identified are encoded near to a recognizable gene for component I (in pfam07307). This enzyme acts in menaquinone-7 isoprenoid side chain biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 131795  Cd Length: 319  Bit Score: 187.23  E-value: 3.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782   1 MFEPVRAELARVEREFAKHLESRVELIPEMGRYVQMSGGKRVRPAVLLMAARLCGYTGDlAVLNAAV-VEFVHTATLVHD 79
Cdd:TIGR02748   5 IYSFLQKDIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLD-AIKHVAVaLELIHMASLVHD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  80 DIIDSAETRRGRLTAHSRWGSDITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHF 159
Cdd:TIGR02748  84 DVIDDADLRRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 160 EIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILML 239
Cdd:TIGR02748 164 RRIKRKTALLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAM 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 240 QRAGAegEQAVLPVIADgqVTPEQWRTIRDLLERHGAIDAAFERAVRHADRAkQHLLEAFPASAERDSLVALADYVIHRD 319
Cdd:TIGR02748 244 EDPFL--KKRIEQVLEE--TTAEEMEPLIEEVKKSDAIEYAYAVSDRYLKKA-LELLDGLPDGRAKKPLQEIAKYIGKRK 318
PLN02857 PLN02857
octaprenyl-diphosphate synthase
37-318 1.46e-48

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 167.72  E-value: 1.46e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  37 SGGKRVRPAVLLMAARLcgyTGDLAVLN---------AAVVEFVHTATLVHDDIIDSAETRRGRLTAHSRWGSDITVLLG 107
Cdd:PLN02857  133 AGGKRMRPALVFLVSRA---TAELAGLKelttehrrlAEITEMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAG 209
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 108 DYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTAYLFAGCAEIGGMLGDADSAR 187
Cdd:PLN02857  210 DFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSLFDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSV 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 188 RTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQRagaegEQAVLPVIADGQVTPEQWRTI 267
Cdd:PLN02857  290 KEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAKGNLTAPVIFALEK-----EPELREIIESEFCEEGSLEEA 364
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1063946782 268 RDLLERHGAIDAAFERAVRHADRAKQHlLEAFPASAERDSLVALADYVIHR 318
Cdd:PLN02857  365 IELVNEGGGIERAQELAKEKADLAIQN-LECLPRGAFRSSLEDMVDYNLER 414
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
65-317 5.40e-45

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: 153.42  E-value: 5.40e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  65 AAVVEFVHTATLVHDDIIDSAETRRGRLTAH---SRWGSDITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGE 141
Cdd:cd00385    16 RAAVEKLHAASLVHDDIVDDSGTRRGLPTAHlavAIDGLPEAILAGDLLLADAFEELAREGSPEALEILAEALLDLLEGQ 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 142 LYQLTKTGDAAITEAEHFEIIRHKTAYLFAGCAEIGGMLGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLgkp 221
Cdd:cd00385    96 LLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRALGLAFQLTNDLLDYEGDAERG--- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 222 lggdlrEGKVTLPIILMLQRAGAEGEQavlpviadgqvtpeqwrtirDLLERHGAIDAAFERAVRHADRAKQHLLEAFPA 301
Cdd:cd00385   173 ------EGKCTLPVLYALEYGVPAEDL--------------------LLVEKSGSLEEALEELAKLAEEALKELNELILS 226
                         250
                  ....*....|....*..
gi 1063946782 302 -SAERDSLVALADYVIH 317
Cdd:cd00385   227 lPDVPRALLALALNLYR 243
PLN02890 PLN02890
geranyl diphosphate synthase
39-320 1.08e-32

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 125.42  E-value: 1.08e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  39 GKRVRPAVLLMAARLCGY-------TGDLAVLN----------AAVVEFVHTATLVHDDIIDSAETRRGRLTAHSRWGSD 101
Cdd:PLN02890  124 GKRFRPTVLLLMATALNVplpesteGGVLDIVAselrtrqqniAEITEMIHVASLLHDDVLDDADTRRGVGSLNVVMGNK 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 102 ITVLLGDYLYIRSMAMALSQGNIEVVRLLCDCTLRLIEGELYQLTKTGDAAITEAEHFEIIRHKTAYLFA-GCAEIGGML 180
Cdd:PLN02890  204 LSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLISnSCKAVAILA 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 181 GDADSARRTALrEYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQragaEGEQaVLPVIADGQVT 260
Cdd:PLN02890  284 GQTAEVAVLAF-EYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAME----EFPQ-LREVVDRGFDN 357
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063946782 261 PEQWRTIRDLLERHGAIDAAFERAVRHADRAKQhLLEAFPASAERD------SLVALADYVIHRDR 320
Cdd:PLN02890  358 PANVDIALEYLGKSRGIQRTRELAREHANLAAA-AIESLPETDDEDvltsrrALIDLTERVITRNK 422
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
29-320 7.19e-20

(2E,6E)-farnesyl diphosphate synthase;


Pssm-ID: 182567  Cd Length: 299  Bit Score: 87.90  E-value: 7.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  29 EMGRYVQMSGGKRVRPAVLLMAARLCGYTGDLAVLNAAVVEFVHTATLVHDDI--IDSAETRRGRLTAHSRWGSDITVLL 106
Cdd:PRK10581   34 EAMQYGALLGGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIHDDLpaMDDDDLRRGLPTCHVKFGEANAILA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 107 GDYLYIRSMAMaLSQGNIEVVrllCDCTLRLIEGELYQLTKT-----GDAAITEAEHFE--------IIRHKTAYLFAGC 173
Cdd:PRK10581  114 GDALQTLAFSI-LSDAPMPEV---SDRDRISMISELASASGIagmcgGQALDLEAEGKQvpldalerIHRHKTGALIRAA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 174 AEIGGM-LGDADSARRTALREYGFDLGIAFQIVDDVLDYTADETTLGKPLGGDLREGKVTLPIILMLQRAGAEGeqavlp 252
Cdd:PRK10581  190 VRLGALsAGDKGRRALPVLDRYAESIGLAFQVQDDILDVVGDTATLGKRQGADQQLGKSTYPALLGLEQARKKA------ 263
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063946782 253 viadgqvtpeqwrtiRDLLerhgaidaaferavrhaDRAKQHLLEAFPASAERDSLVALADYVIHRDR 320
Cdd:PRK10581  264 ---------------RDLI-----------------DDARQSLDQLAAQSLDTSALEALANYIIQRDK 299
hexpp_archaea NF040936
hexaprenyl pyrophosphate synthase;
29-211 1.82e-12

hexaprenyl pyrophosphate synthase;


Pssm-ID: 468868  Cd Length: 275  Bit Score: 66.24  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782  29 EMGRYVqMSGGKRVRpAVLLM--AARLCG-----YTGDLAVlnaavvEFVHTATLVHDDIIDSAETRRGRLTAHSRWGSD 101
Cdd:NF040936   32 EMSKYI-MKDGKRFR-GTLMFlfTEALGGeekdaYKGALAT------EILHSASLALDDIVDYDLTRRGDKSAWAVYTNR 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063946782 102 ITVLLGDYLYIRSMAMALSQGnievvrllcDCTLRlIEGELYQLTKTG---DAAITEAEHFEIIRHKTAYLFagcaEIGG 178
Cdd:NF040936  104 RVIFVSNYLIPTALNIISSYG---------EDALK-ISIELWKDTAVGalkDMYGNKEDYFKTIELKTASLF----KLST 169
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1063946782 179 MLGdADSARRTA----LREYGFDLGIAFQIVDDVLDY 211
Cdd:NF040936  170 MLA-SFSSRREElldeLLDAGKYLGIIYQLIDDYVDC 205
 
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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