|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03201 |
PLN03201 |
RAB geranylgeranyl transferase beta-subunit; Provisional |
10-328 |
0e+00 |
|
RAB geranylgeranyl transferase beta-subunit; Provisional
Pssm-ID: 215630 [Multi-domain] Cd Length: 316 Bit Score: 604.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 10 EAGPRSTLLVDKHATYIKSFSRlwdTPDKLEFVATEHFWMSGMYWGLSAMYLMGRLGDMDRDAILGWVMRCQHTNGGFGG 89
Cdd:PLN03201 1 TSGPMGELVVDKHVRYIKSLEK---KKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 90 SERNDPHLLYTLSAVQILALYDRLDDVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILGRTAAINVPSA 169
Cdd:PLN03201 78 NTGHDPHILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 170 LDFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSGGLNGRPEKLQDVCYSWWCLS 249
Cdd:PLN03201 158 VDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159463140 250 CLSILGRLHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLMGYPNLAAIDPTWALPVEVVERIKRR 328
Cdd:PLN03201 238 SLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
|
|
| GGTase-II |
cd02894 |
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ... |
17-303 |
1.21e-167 |
|
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.
Pssm-ID: 239224 [Multi-domain] Cd Length: 287 Bit Score: 467.90 E-value: 1.21e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 17 LLVDKHATYIKSfsrLWDTPDKLEFVATEHFWMSGMYWGLSAMYLMGRLGDMDRDAILGWVMRCQ-HTNGGFGGSERNDP 95
Cdd:cd02894 1 LLLEKHIEYILS---LTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 96 HLLYTLSAVQILALYDRLD--DVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILGRTAAINVPSALDFI 173
Cdd:cd02894 78 HILSTLSAIQILALYDLLNkiDENKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 174 AKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSGGLNGRPEKLQDVCYSWWCLSCLSI 253
Cdd:cd02894 158 LSCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 159463140 254 LGRLHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLM 303
Cdd:cd02894 238 IGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
70-304 |
1.18e-33 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 124.82 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 70 RDAILGWVMRCQHTNGGFGGSErNDPHLLYTLSAVQILALYDrLDDVDADKVAAYVAGLQRPDGSFA-GDAWGEIDTRFT 148
Cdd:COG5029 21 TDSHLDYLRASQNPDGGFAGRS-GPSDLYSTYYAVRTLALLG-ESPKWRDRVADLLSSLRVEDGGFAkAPEGGAGSTYHT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 149 YCALLCLSILGRtaAINVPSAL-DFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTK 227
Cdd:COG5029 99 YLATLLAELLGR--PPPDPDRLvRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159463140 228 SGGLNGRPEK-LQDVCYSWWCLSCLSILGRlHWIDRSALTTFILDCQdEEDGGISDRP-DDMADVYHTFFGIAGLSLMG 304
Cdd:COG5029 177 EGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQ-LPDGGFEGAPwDGVEDVEYTFYGVGALALLG 253
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
212-255 |
1.65e-10 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 55.60 E-value: 1.65e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 159463140 212 VDRDLFCWWLCERQTKSGGLNGRPEKLQDVCYSWWCLSCLSILG 255
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
70-184 |
7.89e-04 |
|
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 41.27 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 70 RDAiLGWVMRCQHTNGGFGGSE-RNDPHLLYTL--------------------SAVQILALYD-RLDDVDA--DKVAAYV 125
Cdd:TIGR01787 391 RDA-VNWILGMQSSNGGFAAYDpDNTGEWLELLnpsevfgdimidppyvdvtaRVIQALGAFGhRADEIRNvlERALEYL 469
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 159463140 126 AGLQRPDGSFAGdAWGeidTRFTYCALLCLSIL---GRT--AAINVPSALDFIAKCKNFDGGFG 184
Cdd:TIGR01787 470 RREQRADGSWFG-RWG---VNYTYGTGFVLSALaaaGRTyrNCPEVQKACDWLLSRQMPDGGWG 529
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN03201 |
PLN03201 |
RAB geranylgeranyl transferase beta-subunit; Provisional |
10-328 |
0e+00 |
|
RAB geranylgeranyl transferase beta-subunit; Provisional
Pssm-ID: 215630 [Multi-domain] Cd Length: 316 Bit Score: 604.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 10 EAGPRSTLLVDKHATYIKSFSRlwdTPDKLEFVATEHFWMSGMYWGLSAMYLMGRLGDMDRDAILGWVMRCQHTNGGFGG 89
Cdd:PLN03201 1 TSGPMGELVVDKHVRYIKSLEK---KKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 90 SERNDPHLLYTLSAVQILALYDRLDDVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILGRTAAINVPSA 169
Cdd:PLN03201 78 NTGHDPHILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 170 LDFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSGGLNGRPEKLQDVCYSWWCLS 249
Cdd:PLN03201 158 VDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLS 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159463140 250 CLSILGRLHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLMGYPNLAAIDPTWALPVEVVERIKRR 328
Cdd:PLN03201 238 SLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
|
|
| GGTase-II |
cd02894 |
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ... |
17-303 |
1.21e-167 |
|
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.
Pssm-ID: 239224 [Multi-domain] Cd Length: 287 Bit Score: 467.90 E-value: 1.21e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 17 LLVDKHATYIKSfsrLWDTPDKLEFVATEHFWMSGMYWGLSAMYLMGRLGDMDRDAILGWVMRCQ-HTNGGFGGSERNDP 95
Cdd:cd02894 1 LLLEKHIEYILS---LTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 96 HLLYTLSAVQILALYDRLD--DVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILGRTAAINVPSALDFI 173
Cdd:cd02894 78 HILSTLSAIQILALYDLLNkiDENKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 174 AKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSGGLNGRPEKLQDVCYSWWCLSCLSI 253
Cdd:cd02894 158 LSCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKI 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 159463140 254 LGRLHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLM 303
Cdd:cd02894 238 IGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
|
|
| PTase |
cd02890 |
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ... |
20-303 |
2.79e-133 |
|
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes.
Pssm-ID: 239220 [Multi-domain] Cd Length: 286 Bit Score: 380.78 E-value: 2.79e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 20 DKHATYIKSfsrlWDTPDKLEFVATEHFWMSGMYWGLSAMYLMGR-LGDMDRDAILGWVMRCQ-HTNGGFGGSERNDPHL 97
Cdd:cd02890 2 EKHIKYLQR----CLKLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 98 LYTLSAVQILALY--DRLDDVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILGRTAAINVPSALDFIAK 175
Cdd:cd02890 78 ASTYAAVLSLAILgdDALSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 176 CKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSG-GLNGRPEKLQDVCYSWWCLSCLSIL 254
Cdd:cd02890 158 CQNYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKIL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 159463140 255 GRLHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLM 303
Cdd:cd02890 238 GRLHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
|
|
| GGTase-I |
cd02895 |
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ... |
19-303 |
7.44e-69 |
|
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I ). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity.
Pssm-ID: 239225 [Multi-domain] Cd Length: 307 Bit Score: 217.53 E-value: 7.44e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 19 VDKHATYIKSFSRLWdtPDKLEFVATEHfwMSGMYWGLSAMYLMGRL---GDMDRDAILGWVMRCQ----HTNGGFGGSE 91
Cdd:cd02895 1 KKKHVKFFQRCLQLL--PSSYQSLDTNR--LTIAFFALSGLDLLGALdsiLVEEKDDIIEWIYSLQvlsnLPRGGFRGSS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 92 ----------RNDPHLLYTLSAVQILA-LYDRLDDVDADKVAAYVAGLQRPDGSFAGDAW---GEIDTRFTYCALLCLSI 157
Cdd:cd02895 77 tlglpgtaskYDTGNLAMTYFALLSLLiLGDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 158 LG--RTAAINVPSALDFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALH---LVDRDLFCWWLCERQTKSGGLN 232
Cdd:cd02895 157 LDdwSEEDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEelsEKFLERLKRWLVHRQVSGTGFN 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159463140 233 GRPEKLQDVCYSWWCLSCLSILGRLHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLM 303
Cdd:cd02895 237 GRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
|
|
| FTase |
cd02893 |
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ... |
20-302 |
3.08e-64 |
|
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a subgroup of PTase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. These proteins are heterodimers of alpha and beta subunits. Both subunits are required for catalytic activity. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids. Ftase attaches a 15-carbon farnesyl group to the cysteine within the C-terminal CaaX motif of substrate proteins when X is Ala, Met, Ser, Cys or Gln. Protein farnesylation has been shown to play critical roles in a variety of cellular processes including Ras/mitogen activated protein kinase signaling pathways in mammals and, abscisic acid signal transduction in Arabidopsis.
Pssm-ID: 239223 [Multi-domain] Cd Length: 299 Bit Score: 205.55 E-value: 3.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 20 DKHATYIKSFsrLWDTPDKLEFVATEHFWMsgMYWGLSAMYLMGRLGDMD-RDAILGWVMRCQHTNGGFGGSERNDPHLL 98
Cdd:cd02893 2 EKHIKYLKKS--LRQLPSSFTSLDASRPWL--LYWILHSLELLGEELDQSyADDVISFLRRCQNPSGGFGGGPGQLPHLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 99 YTLSAVQILAL---YDRLDDVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILGRTAAINVPSALDFIAK 175
Cdd:cd02893 78 TTYAAVNALAIigtEEAYDVIDREALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 176 CKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKS-GGLNGRPEKLQDVCYSWWCLSCLSIL 254
Cdd:cd02893 158 CQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPIL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159463140 255 GRL------------HW-IDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSL 302
Cdd:cd02893 238 EAIlnaekkfddsaeGTlFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
19-303 |
6.30e-64 |
|
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two broadly specific proteinase inhibitors alpha2-macroglobulin (alpha (2)-M) and pregnancy zone protein (PZP) and, the C3 C4 and C5 components of vertebrate complement. Class II terpene cyclases include squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY), these integral membrane proteins catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. The protein prenyltransferases include protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II) which catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Alpha (2)-M is a major carrier protein in serum and involved in the immobilization and entrapment of proteases. PZP is a pregnancy associated protein. Alpha (2)-M and PZP are known to bind to and, may modulate, the activity of placental protein-14 in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system.
Pssm-ID: 238362 [Multi-domain] Cd Length: 300 Bit Score: 204.71 E-value: 6.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 19 VDKHATYIKSFsrlwDTPDKLEFVATEHFWMSGMYWGLSAMYLMGR------LGDMDRDAILGWVMRCQHTNGGFGGSER 92
Cdd:cd00688 1 IEKHLKYLLRY----PYGDGHWYQSLCGEQTWSTAWPLLALLLLLAatgirdKADENIEKGIQRLLSYQLSDGGFSGWGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 93 ND-PHLLYTLSAVQILALYDRLDDVDAD---KVAAYVAGLQRPDGSFAGDAWG-------EIDTRFTYCALLCLSILGR- 160
Cdd:cd00688 77 NDyPSLWLTAYALKALLLAGDYIAVDRIdlaRALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 161 TAAINVPSALDFIAKCKNFDGGFGctPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSGGLNGRPE---K 237
Cdd:cd00688 157 DPDPLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnK 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 159463140 238 LQDVCYSWWCLSCLSILGRL-HWIDRSALTTFILDCQDeEDGGISDRPDDMADVYHTFFGIAGLSLM 303
Cdd:cd00688 235 LSDSCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
70-304 |
1.18e-33 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 124.82 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 70 RDAILGWVMRCQHTNGGFGGSErNDPHLLYTLSAVQILALYDrLDDVDADKVAAYVAGLQRPDGSFA-GDAWGEIDTRFT 148
Cdd:COG5029 21 TDSHLDYLRASQNPDGGFAGRS-GPSDLYSTYYAVRTLALLG-ESPKWRDRVADLLSSLRVEDGGFAkAPEGGAGSTYHT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 149 YCALLCLSILGRtaAINVPSAL-DFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTK 227
Cdd:COG5029 99 YLATLLAELLGR--PPPDPDRLvRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159463140 228 SGGLNGRPEK-LQDVCYSWWCLSCLSILGRlHWIDRSALTTFILDCQdEEDGGISDRP-DDMADVYHTFFGIAGLSLMG 304
Cdd:COG5029 177 EGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQ-LPDGGFEGAPwDGVEDVEYTFYGVGALALLG 253
|
|
| PLN02710 |
PLN02710 |
farnesyltranstransferase subunit beta |
4-305 |
8.07e-32 |
|
farnesyltranstransferase subunit beta
Pssm-ID: 215380 [Multi-domain] Cd Length: 439 Bit Score: 123.74 E-value: 8.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 4 AGTGPAEAGPRSTLLVDKHATYI-KSFSRLwdtPDKLEFVATEHFWMSgmYWGLSAMYLMGR-LGD-MDRDAIlGWVMRC 80
Cdd:PLN02710 31 ASAPPNAQSVMLELWREKHLEYLtRGLRQL---GPSFSVLDANRPWLC--YWILHSIALLGEsLDDeLENDTI-DFLSRC 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 81 QHTNGGFGGSERNDPHLLYTLSAVQILALY--DR-LDDVDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSI 157
Cdd:PLN02710 105 QDPNGGYGGGPGQLPHLATTYAAVNTLVTIggERaLSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 158 LGrtaaINVPSAL----DFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWWLCERQTKSGGLNG 233
Cdd:PLN02710 185 LN----ILDDELVkgvgDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVEGGFQG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 234 RPEKLQDVCYSWWCLSCLSILGRLHWI----------------------------------------------------- 260
Cdd:PLN02710 261 RTNKLVDGCYSFWQGGVFALLQQLVTIvdeqlqtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnq 340
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 159463140 261 ------DRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLMGY 305
Cdd:PLN02710 341 qmgplfHSIALQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLSVAQY 391
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
56-187 |
9.92e-19 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 84.39 E-value: 9.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 56 LSAMYLMGRLG------DMDRDAILGWVMRCQHTNGGFGGSernDPHLLYTLSAVQILALYDRlDDVDADKVAAYVAGLQ 129
Cdd:COG1689 117 LEETYLAVALLealgasEPEREKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQ 192
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 130 RPDGSF--AGDAWGEIDTrfTYCALLCLSILGRTAaINVPSALDFIAKCKNFDGGFGCTP 187
Cdd:COG1689 193 NEDGGFskTPGSYSDLEA--TYYALRALKLLGEPP-KNVDKLLEFIASCQNSDGGFRRSP 249
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
62-306 |
4.68e-17 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 79.77 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 62 MGRLgDMDRDAILGWVMRCQHTNGGFGGSERNDPHLLYTLSAVQILALYD-RLDDVdaDKVAAYVAGLQRPDGSFAGdaw 140
Cdd:COG1689 1 MTSL-RFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLGeEVPNR--DKTIEFLESCQDEEGGGFA--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 141 geidTRFTYCALLCLSILGRTaainvPSALDFIAKcKNFDGGFGCTPGNESHAGQVFTCIGALSLANALHLVDRDLFCWW 220
Cdd:COG1689 75 ----LYTTSYGLMALALLGID-----PPDEQEALE-YLSDALPTKFAGGASDLEETYLAVALLEALGASEPEREKIREFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 221 LcERQTKSGGLNGRPEKLQDvcySWWCLSCLSILGRlHWIDRSALTTFILDCQDeEDGGISDRPDDMADVYHTFFGIAGL 300
Cdd:COG1689 145 L-SLRRPDGGFGGKKPNLED---TYWALAALRRLGR-DLPPADRVIAFILACQN-EDGGFSKTPGSYSDLEATYYALRAL 218
|
....*.
gi 159463140 301 SLMGYP 306
Cdd:COG1689 219 KLLGEP 224
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
53-209 |
3.42e-15 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 74.36 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 53 YWGLSAMYLMGRlGDMDRDAILGWVMRCQHTNGGFGGSERNDPHLLYTLSAVQILALYDRLDDVDADKVAAYVAGLQRPD 132
Cdd:COG5029 99 YLATLLAELLGR-PPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPE 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 159463140 133 GSF-AGDAWGEIDTRFTYCALLCLSILGRtAAINVPSALDFIAKCKNFDGGFGCTPGNES-HAGQVFTCIGALSLANAL 209
Cdd:COG5029 178 GGFaYNTRIGEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPDGGFEGAPWDGVeDVEYTFYGVGALALLGAL 255
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
168-307 |
1.23e-11 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 63.96 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 168 SALDFIAKCKNFDGGFGCTPGnESHAGQVFTCIGALSLANALHlVDRDLFCWWLCERQTKSGGLNGRPEKLQDVCY-SWW 246
Cdd:COG5029 23 SHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESP-KWRDRVADLLSSLRVEDGGFAKAPEGGAGSTYhTYL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 159463140 247 CLSCLSILGRlHWIDRSALTTFILDCQDEeDGGISDRPDDMADVYHTFFGIAGLSLMGYPN 307
Cdd:COG5029 101 ATLLAELLGR-PPPDPDRLVRFLISQQND-DGGFEISPGRRSDTNPTAAAIGALRALGALD 159
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
212-255 |
1.65e-10 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 55.60 E-value: 1.65e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 159463140 212 VDRDLFCWWLCERQTKSGGLNGRPEKLQDVCYSWWCLSCLSILG 255
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
116-159 |
2.35e-10 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 55.21 E-value: 2.35e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 159463140 116 VDADKVAAYVAGLQRPDGSFAGDAWGEIDTRFTYCALLCLSILG 159
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
260-304 |
8.05e-09 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 50.97 E-value: 8.05e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 159463140 260 IDRSALTTFILDCQDEeDGGISDRPDDMADVYHTFFGIAGLSLMG 304
Cdd:pfam00432 1 IDKEKLVDYLLSCQNE-DGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
164-207 |
1.16e-08 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 50.20 E-value: 1.16e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 159463140 164 INVPSALDFIAKCKNFDGGFGCTPGNESHAGQVFTCIGALSLAN 207
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
68-111 |
4.32e-08 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 48.66 E-value: 4.32e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 159463140 68 MDRDAILGWVMRCQHTNGGFGGSERNDPHLLYTLSAVQILALYD 111
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
53-162 |
2.98e-07 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 50.86 E-value: 2.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 53 YWGLSAMYLMGRLGDMDRDAILGWVMRCQHTNGGFGGSERN-DPHLLYTLSAVQILALYDRLDDVDADKVAaYVAGLQRP 131
Cdd:COG5029 146 AAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGAAPKLVDDLQA-YILSLQLP 224
|
90 100 110
....*....|....*....|....*....|..
gi 159463140 132 DGSFAGDAWGEI-DTRFTYCALLCLSILGRTA 162
Cdd:COG5029 225 DGGFEGAPWDGVeDVEYTFYGVGALALLGALA 256
|
|
| PTase |
cd02890 |
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ... |
246-312 |
9.14e-07 |
|
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes.
Pssm-ID: 239220 [Multi-domain] Cd Length: 286 Bit Score: 49.50 E-value: 9.14e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 159463140 246 WCLSCLSILGR-LHWIDRSALTTFILDCQDEEDGGISDRPDDMADVYHTFFGIAGLSLMGYPNLAAID 312
Cdd:cd02890 32 WILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSLAILGDDALSRID 99
|
|
| SQCY |
cd02889 |
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ... |
68-184 |
3.34e-04 |
|
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.
Pssm-ID: 239219 [Multi-domain] Cd Length: 348 Bit Score: 41.82 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 68 MDRDAI---LGWVMRCQHTNGGFGGSER-NDPHLLY------------------TLSAVQILALYDRLDD---VDADKVA 122
Cdd:cd02889 114 VSRERLydaVDWLLSMQNSNGGFAAFEPdNTYKYLElipevdgdimidppyvecTGSVLEALGLFGKLYPehrREIDPAI 193
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 123 A----YVAGLQRPDGSFAGdAWGeidTRFTY---CALLCLSILGRTAAIN-VPSALDFIAKCKNFDGGFG 184
Cdd:cd02889 194 RravkYLEREQEPDGSWYG-RWG---VCFIYgtwFALEALAAAGEDENSPyVRKACDWLLSKQNPDGGWG 259
|
|
| SqhC |
COG1657 |
Terpene cyclase SqhC [Lipid transport and metabolism]; |
55-184 |
5.56e-04 |
|
Terpene cyclase SqhC [Lipid transport and metabolism];
Pssm-ID: 441263 [Multi-domain] Cd Length: 644 Bit Score: 41.73 E-value: 5.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 55 GLSAMYLMGRLGDMD-RDAI---LGWVMRCQHTNGGFGGSER-NDPHLLY------------------TLSAVQILALYD 111
Cdd:COG1657 396 VLMALLRLRLPDEPRyREAIeraVEWILGMQSRDGGWGAFDKdNTKEWLNkipfadhgalldpptadvTARCLEMLGQLG 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 112 RLDDVDA-DKVAAYVAGLQRPDGSFAGdAWGeidTRFTY------CALlclsilgrtAAINVPS-------ALDFIAKCK 177
Cdd:COG1657 476 LTEDHPAiRRAVAYLRREQEPDGSWFG-RWG---VNYIYgtwsvlTGL---------NAAGVDPddpairrAVAWLLSIQ 542
|
....*..
gi 159463140 178 NFDGGFG 184
Cdd:COG1657 543 NADGGWG 549
|
|
| SQCY_1 |
cd02892 |
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ... |
68-184 |
7.11e-04 |
|
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.
Pssm-ID: 239222 [Multi-domain] Cd Length: 634 Bit Score: 41.41 E-value: 7.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 68 MDRDAI---LGWVMRCQHTNGGFGGSER-NDPHLLYTL--------------------SAVQILALYDRLDD---VDADK 120
Cdd:cd02892 397 VSRERLydaVDWLLGMQNSNGGFAAFEPdNTYHWLENLnpfedfgdimidppyvectgSVLEALGLFGKLYPghrREIDP 476
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 159463140 121 VAA----YVAGLQRPDGSFAGdAWGeidTRFTY---CALLCLSILGRT----AAINvpSALDFIAKCKNFDGGFG 184
Cdd:cd02892 477 AIRravkYLLREQEPDGSWYG-RWG---VCYIYgtwFALEALAAAGEDyensPYIR--KACDFLLSKQNPDGGWG 545
|
|
| squalene_cyclas |
TIGR01787 |
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ... |
70-184 |
7.89e-04 |
|
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.
Pssm-ID: 273809 [Multi-domain] Cd Length: 621 Bit Score: 41.27 E-value: 7.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 159463140 70 RDAiLGWVMRCQHTNGGFGGSE-RNDPHLLYTL--------------------SAVQILALYD-RLDDVDA--DKVAAYV 125
Cdd:TIGR01787 391 RDA-VNWILGMQSSNGGFAAYDpDNTGEWLELLnpsevfgdimidppyvdvtaRVIQALGAFGhRADEIRNvlERALEYL 469
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 159463140 126 AGLQRPDGSFAGdAWGeidTRFTYCALLCLSIL---GRT--AAINVPSALDFIAKCKNFDGGFG 184
Cdd:TIGR01787 470 RREQRADGSWFG-RWG---VNYTYGTGFVLSALaaaGRTyrNCPEVQKACDWLLSRQMPDGGWG 529
|
|
| |
