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Conserved domains on  [gi|1437908453|emb|SUF20717|]
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octaprenyl diphosphate synthase [Salmonella enterica]

Protein Classification

octaprenyl-diphosphate synthase( domain architecture ID 10793493)

octaprenyl-diphosphate synthase (all-trans) catalyzes consecutive condensation reactions of one allylic substrate farnesyl pyrophosphate (FPP) and five homoallylic substrate isopentenyl pyrophosphate (IPP) molecules to form a C40 long-chain product OPP, which serves as a side chain of ubiquinone and menaquinone

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
176-498 0e+00

octaprenyl diphosphate synthase; Provisional


:

Pssm-ID: 182813  Cd Length: 323  Bit Score: 690.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 176 MNLEKINELTAQDMAGVNATILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 255
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 256 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 335
Cdd:PRK10888   81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 336 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPL 415
Cdd:PRK10888  161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 416 LHAMRHGTPEQSTMIRTAIEQGNGRHLLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQ 495
Cdd:PRK10888  241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                  ...
gi 1437908453 496 RDR 498
Cdd:PRK10888  321 RDR 323
 
Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
176-498 0e+00

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 690.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 176 MNLEKINELTAQDMAGVNATILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 255
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 256 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 335
Cdd:PRK10888   81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 336 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPL 415
Cdd:PRK10888  161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 416 LHAMRHGTPEQSTMIRTAIEQGNGRHLLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQ 495
Cdd:PRK10888  241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                  ...
gi 1437908453 496 RDR 498
Cdd:PRK10888  321 RDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
176-498 2.38e-152

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: 437.35  E-value: 2.38e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 176 MNLEKINELTAQDMAGVNATILEQLN-SDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTA 254
Cdd:COG0142     1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 255 TLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGS----LKVLEVMSEAVNVIAEGEVLQLMNVND 330
Cdd:COG0142    81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 331 PDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGK 410
Cdd:COG0142   161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 411 PTLPLLHAMRHGTPEQSTMIRTAIEQGN-GRHLLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGL 489
Cdd:COG0142   241 PTLPLLLALERADPEERAELRELLGKPDlDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                  ....*....
gi 1437908453 490 AHIAVQRDR 498
Cdd:COG0142   321 ADYVVERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
202-496 3.66e-107

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: 319.50  E-value: 3.66e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 202 SDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQG-NAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGN 280
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPElEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 281 AASVLVGDFIYTRAFQMMTSLGS---LKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 357
Cdd:cd00685    81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 358 GILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMrhgtpeqstmirtaieqg 437
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1437908453 438 ngrhlldpvleamttcgslewtRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQR 496
Cdd:cd00685   223 ----------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
204-438 1.63e-100

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 302.12  E-value: 1.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 204 VQLINQLGYYIISGGGKRIRPMIAVLAARAVG--YQGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNA 281
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 282 ASVLVGDFIYTRAFQMMTSL-GSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDI--TEENYMRVIYSKTARLFEAAAQCSG 358
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 359 ILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMRHgTPEQSTMIRTAIEQGN 438
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
188-497 7.72e-63

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: 207.26  E-value: 7.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 188 DMAGVNATILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDM 267
Cdd:TIGR02748  12 DIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDADL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 268 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 347
Cdd:TIGR02748  92 RRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 348 RLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMRHGTPEQS 427
Cdd:TIGR02748 172 LLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKR 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 428 tmIRTAIEQGNGRHlLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQRD 497
Cdd:TIGR02748 252 --IEQVLEETTAEE-MEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRK 318
 
Name Accession Description Interval E-value
PRK10888 PRK10888
octaprenyl diphosphate synthase; Provisional
176-498 0e+00

octaprenyl diphosphate synthase; Provisional


Pssm-ID: 182813  Cd Length: 323  Bit Score: 690.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 176 MNLEKINELTAQDMAGVNATILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 255
Cdd:PRK10888    1 MNLEKINELTAQDMAGVNAAILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTAT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 256 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 335
Cdd:PRK10888   81 LLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 336 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPL 415
Cdd:PRK10888  161 ENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGETLGKNVGDDLNEGKPTLPL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 416 LHAMRHGTPEQSTMIRTAIEQGNGRHLLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQ 495
Cdd:PRK10888  241 LHAMHHGTPEQAAMIRTAIEQGNGRHLLEPVLEAMNACGSLEWTRQRAEEEADKAIAALQVLPDTPWREALIGLAHIAVQ 320

                  ...
gi 1437908453 496 RDR 498
Cdd:PRK10888  321 RDR 323
IspA COG0142
Geranylgeranyl pyrophosphate synthase [Coenzyme transport and metabolism]; Geranylgeranyl ...
176-498 2.38e-152

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: 437.35  E-value: 2.38e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 176 MNLEKINELTAQDMAGVNATILEQLN-SDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTA 254
Cdd:COG0142     1 MTLKDLLALLAEDLARVEAALEELLArSEPPLLAEAMRYLLLAGGKRLRPLLVLLAARALGGDPEAALRAAAAVELIHTA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 255 TLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGS----LKVLEVMSEAVNVIAEGEVLQLMNVND 330
Cdd:COG0142    81 SLVHDDVMDDDDLRRGKPTVHARFGEATAILAGDALLALAFELLAELGDperrLRALRILARAARGMCEGQALDLEAEGR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 331 PDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGK 410
Cdd:COG0142   161 LDVTLEEYLRVIRLKTAALFAAALRLGAILAGADEEQVEALRRYGRNLGLAFQIRDDILDVTGDPEVLGKPAGSDLREGK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 411 PTLPLLHAMRHGTPEQSTMIRTAIEQGN-GRHLLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGL 489
Cdd:COG0142   241 PTLPLLLALERADPEERAELRELLGKPDlDEEDLAEVRALLRESGALEYARELARELAEEALAALAALPDSEAREALRAL 320

                  ....*....
gi 1437908453 490 AHIAVQRDR 498
Cdd:COG0142   321 ADYVVERDR 329
Trans_IPPS_HT cd00685
Trans-Isoprenyl Diphosphate Synthases, head-to-tail; These trans-Isoprenyl Diphosphate ...
202-496 3.66e-107

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: 319.50  E-value: 3.66e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 202 SDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQG-NAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGN 280
Cdd:cd00685     1 SEVELLREALRYLLLAGGKRLRPLLVLLAARALGGPElEAALRLAAAIELLHTASLVHDDVMDNSDLRRGKPTVHKVFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 281 AASVLVGDFIYTRAFQMMTSLGS---LKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 357
Cdd:cd00685    81 ATAILAGDYLLARAFELLARLGNpyyPRALELFSEAILELVEGQLLDLLSEYDTDVTEEEYLRIIRLKTAALFAAAPLLG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 358 GILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMrhgtpeqstmirtaieqg 437
Cdd:cd00685   161 ALLAGADEEEAEALKRFGRNLGLAFQIQDDILDLFGDPETLGKPVGSDLREGKCTLPVLLAL------------------ 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1437908453 438 ngrhlldpvleamttcgslewtRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQR 496
Cdd:cd00685   223 ----------------------RELAREYEEKALEALKALPESPAREALRALADFILER 259
polyprenyl_synt pfam00348
Polyprenyl synthetase;
204-438 1.63e-100

Polyprenyl synthetase;


Pssm-ID: 459773  Cd Length: 251  Bit Score: 302.12  E-value: 1.63e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 204 VQLINQLGYYIISGGGKRIRPMIAVLAARAVG--YQGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANAAFGNA 281
Cdd:pfam00348   1 EKLLYEPLDYLVSAGGKRIRPLLVLLSAEALGgpEDLEKAIVLAWAVELLHAASLVHDDIMDNSDLRRGQPTWHRIFGNA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 282 ASVLVGDFIYTRAFQMMTSL-GSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDI--TEENYMRVIYSKTARLFEAAAQCSG 358
Cdd:pfam00348  81 IAINDGDYLYALAFQLLAKLfPNPELLELFSEVTLQTAEGQGLDLLWRNDDDLscTEEEYLEIVKYKTAYLFALAVKLGA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 359 ILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMRHgTPEQSTMIRTAIEQGN 438
Cdd:pfam00348 161 ILSGADDEVIEALKDYGLNLGLAFQIQDDYLDLFGDPEVLGKPAGTDITEGKCTWPVIHALER-TPEQRKILLEIYGKRP 239
Trans_IPPS cd00867
Trans-Isoprenyl Diphosphate Synthases; Trans-Isoprenyl Diphosphate Synthases (Trans_IPPS) of ...
222-496 3.38e-73

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: 231.46  E-value: 3.38e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 222 IRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDMRRGKATANA-AFGNAASVLVGDFIYTRAFQMMTS 300
Cdd:cd00867     1 SRPLLVLLLARALGGDLEAALRLAAAVELLHAASLVHDDIVDDSDLRRGKPTAHLrRFGNALAILAGDYLLARAFQLLAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 301 LGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGT 380
Cdd:cd00867    81 LGYPRALELFAEALRELLEGQALDLEFERDTYETLDEYLEYCRYKTAGLVGLLCLLGAGLSGADDEQAEALKDYGRALGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 381 AFQLIDDLLDYSADGKHLGKnVGDDLNEGKPTLPLLHAMRhgtpeqstmirtaieqgngrhlldpvleamttcgslewtr 460
Cdd:cd00867   161 AFQLTDDLLDVFGDAEELGK-VGSDLREGRITLPVILARE---------------------------------------- 199
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1437908453 461 qRAEEEADKAISALQILPDTP--WREALIGLAHIAVQR 496
Cdd:cd00867   200 -RAAEYAEEAYAALEALPPSLprARRALIALADFLYRR 236
PLN02857 PLN02857
octaprenyl-diphosphate synthase
175-496 6.72e-63

octaprenyl-diphosphate synthase


Pssm-ID: 215462  Cd Length: 416  Bit Score: 210.47  E-value: 6.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 175 AMNLEKINELTAQDMAGVNATILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGN------AHVTIAALI 248
Cdd:PLN02857   91 PISLSELFEPVADDLQQLNDNLQSIVGAENPVLMSAAEQIFGAGGKRMRPALVFLVSRATAELAGlkelttEHRRLAEIT 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 249 EFIHTATLLHDDVVDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNV 328
Cdd:PLN02857  171 EMIHTASLIHDDVLDESDMRRGKETVHQLYGTRVAVLAGDFMFAQSSWYLANLDNLEVIKLISQVIKDFASGEIKQASSL 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 329 NDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNE 408
Cdd:PLN02857  251 FDCDVTLDEYLLKSYYKTASLIAASTKSAAIFSGVDSSVKEQMYEYGKNLGLAFQVVDDILDFTQSTEQLGKPAGSDLAK 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 409 GKPTLPLLHAMRHgTPEQSTMIRTAI-EQGNgrhlLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALI 487
Cdd:PLN02857  331 GNLTAPVIFALEK-EPELREIIESEFcEEGS----LEEAIELVNEGGGIERAQELAKEKADLAIQNLECLPRGAFRSSLE 405

                  ....*....
gi 1437908453 488 GLAHIAVQR 496
Cdd:PLN02857  406 DMVDYNLER 414
GerC3_HepT TIGR02748
heptaprenyl diphosphate synthase component II; Members of this family are component II of the ...
188-497 7.72e-63

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: 207.26  E-value: 7.72e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 188 DMAGVNATILEQLNSDVQLINQLGYYIISGGGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLHDDVVDESDM 267
Cdd:TIGR02748  12 DIDSIEKELEKAVQAEHPVLSEASLHLLEAGGKRIRPVFVLLAGKFGDYDLDAIKHVAVALELIHMASLVHDDVIDDADL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 268 RRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTA 347
Cdd:TIGR02748  92 RRGRPTIKSKWGNRIAMYTGDYLFAKSLETMTEIKDPRAHQILSHTIVEVCRGEIEQIKDKYNFDQNLRTYLRRIKRKTA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 348 RLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMRHGTPEQS 427
Cdd:TIGR02748 172 LLIAASCQLGAIASGANEAIVKKLYWFGYYVGMSYQITDDILDFVGTEEELGKPAGGDLLQGNVTLPVLYAMEDPFLKKR 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 428 tmIRTAIEQGNGRHlLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQRD 497
Cdd:TIGR02748 252 --IEQVLEETTAEE-MEPLIEEVKKSDAIEYAYAVSDRYLKKALELLDGLPDGRAKKPLQEIAKYIGKRK 318
preA CHL00151
prenyl transferase; Reviewed
196-498 4.78e-59

prenyl transferase; Reviewed


Pssm-ID: 164542  Cd Length: 323  Bit Score: 197.71  E-value: 4.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 196 ILEQ-LNSDVQLINQLGY----YIISGGGKRIRPMIAVLAARAVGyqGNAHVT-----IAALIEFIHTATLLHDDVVDES 265
Cdd:CHL00151   17 ILEDnLKKLIGSGHPILYaaakHLFSAGGKRIRPAIVLLVAKATG--GNMEIKtsqqrLAEITEIIHTASLVHDDVIDEC 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 266 DMRRGKATANAAFGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSK 345
Cdd:CHL00151   95 SIRRGIPTVHKIFGTKIAVLAGDFLFAQSSWYLANLNNLEVVKLISKVITDFAEGEIRQGLVQFDTTLSILNYIEKSFYK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 346 TARLFEAAAQCSGILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMrhgtpE 425
Cdd:CHL00151  175 TASLIAASCKAAALLSDADEKDHNDFYLYGKHLGLAFQIIDDVLDITSSTESLGKPIGSDLKNGNLTAPVLFAL-----T 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1437908453 426 QSTMIRTAIE-QGNGRHLLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDTPWREALIGLAHIAVQRDR 498
Cdd:CHL00151  250 QNSKLAKLIErEFCETKDISQALQIIKETNGIEKAKDLALEHMQAAIQCLKFLPPSSAKDSLIEIANFIINRLN 323
Isoprenoid_Biosyn_C1 cd00385
Isoprenoid Biosynthesis enzymes, Class 1; Superfamily of trans-isoprenyl diphosphate synthases ...
222-491 5.79e-53

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: 179.23  E-value: 5.79e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 222 IRPMIAVLAARAVgyqgnahvTIAALIEFIHTATLLHDDVVDESDMRRGKATANAA---FGNAASVLVGDFIYTRAFQMM 298
Cdd:cd00385     1 FRPLAVLLEPEAS--------RLRAAVEKLHAASLVHDDIVDDSGTRRGLPTAHLAvaiDGLPEAILAGDLLLADAFEEL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 299 TSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGCTPEQEKGLQDYGRYL 378
Cdd:cd00385    73 AREGSPEALEILAEALLDLLEGQLLDLKWRREYVPTLEEYLEYCRYKTAGLVGALCLLGAGLSGGEAELLEALRKLGRAL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 379 GTAFQLIDDLLDYSADGKHLgknvgddlnEGKPTLPLLHAMRHGTPEQstmirtaieqgngrhlldpVLEAMTTCGSLEW 458
Cdd:cd00385   153 GLAFQLTNDLLDYEGDAERG---------EGKCTLPVLYALEYGVPAE-------------------DLLLVEKSGSLEE 204
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1437908453 459 TRQRAEEEADKAISALQILPDTP--WREALIGLAH 491
Cdd:cd00385   205 ALEELAKLAEEALKELNELILSLpdVPRALLALAL 239
PLN02890 PLN02890
geranyl diphosphate synthase
219-498 2.84e-47

geranyl diphosphate synthase


Pssm-ID: 178478  Cd Length: 422  Bit Score: 169.34  E-value: 2.84e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 219 GKRIRPMIAVLAARAVgyqgNAHVT---------------------IAALIEFIHTATLLHDDVVDESDMRRGKATANAA 277
Cdd:PLN02890  124 GKRFRPTVLLLMATAL----NVPLPesteggvldivaselrtrqqnIAEITEMIHVASLLHDDVLDDADTRRGVGSLNVV 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 278 FGNAASVLVGDFIYTRAFQMMTSLGSLKVLEVMSEAVNVIAEGEVLQLMNVNDPDITEENYMRVIYSKTARLFEAAAQCS 357
Cdd:PLN02890  200 MGNKLSVLAGDFLLSRACVALAALKNTEVVSLLATAVEHLVTGETMQITSSREQRRSMDYYMQKTYYKTASLISNSCKAV 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 358 GILAGCTPEQEKGLQDYGRYLGTAFQLIDDLLDYSADGKHLGKNVGDDLNEGKPTLPLLHAMrhgtpEQSTMIRTAIEQG 437
Cdd:PLN02890  280 AILAGQTAEVAVLAFEYGRNLGLAFQLIDDVLDFTGTSASLGKGSLSDIRHGVITAPILFAM-----EEFPQLREVVDRG 354
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1437908453 438 --NGRHlLDPVLEAMTTCGSLEWTRQRAEEEADKAISALQILPDT------PWREALIGLAHIAVQRDR 498
Cdd:PLN02890  355 fdNPAN-VDIALEYLGKSRGIQRTRELAREHANLAAAAIESLPETddedvlTSRRALIDLTERVITRNK 422
PRK10581 PRK10581
(2E,6E)-farnesyl diphosphate synthase;
197-498 1.44e-20

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


Pssm-ID: 182567  Cd Length: 299  Bit Score: 92.14  E-value: 1.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 197 LEQLNSDVQLINQ-LGYYIISG-----------------GGKRIRPMIAVLAARAVGYQGNAHVTIAALIEFIHTATLLH 258
Cdd:PRK10581    4 PQQLQACVQQANQaLSRFIAPLpfqntpvveamqygallGGKRLRPFLVYATGQMFGVSTNTLDAPAAAVECIHAYSLIH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 259 DDV--VDESDMRRGKATANAAFGNAASVLVGDFIYTRAFQM-----MTSLGSLKVLEVMSE-----AVNVIAEGEVLQLm 326
Cdd:PRK10581   84 DDLpaMDDDDLRRGLPTCHVKFGEANAILAGDALQTLAFSIlsdapMPEVSDRDRISMISElasasGIAGMCGGQALDL- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 327 NVNDPDITEENYMRVIYSKTARLFEAAAQCSGILAGctpeqEKG------LQDYGRYLGTAFQLIDDLLDYSADGKHLGK 400
Cdd:PRK10581  163 EAEGKQVPLDALERIHRHKTGALIRAAVRLGALSAG-----DKGrralpvLDRYAESIGLAFQVQDDILDVVGDTATLGK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1437908453 401 NVGDDLNEGKPTLPLLHAmrhgtpeqstmirtaieqgngrhlldpvleamttcgsLEWTRQRAEEEADKAISALQILPDT 480
Cdd:PRK10581  238 RQGADQQLGKSTYPALLG-------------------------------------LEQARKKARDLIDDARQSLDQLAAQ 280
                         330
                  ....*....|....*....
gi 1437908453 481 PWR-EALIGLAHIAVQRDR 498
Cdd:PRK10581  281 SLDtSALEALANYIIQRDK 299
 
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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