|
Name |
Accession |
Description |
Interval |
E-value |
| GGTase-I |
cd02895 |
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ... |
22-332 |
1.30e-172 |
|
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: 483.32 E-value: 1.30e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLD---VVNKDDIIEWIYSLQVLptedrSNLNRCGFRGS 98
Cdd:cd02895 1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDsilVEEKDDIIEWIYSLQVL-----SNLPRGGFRGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 99 SYLGIPfnpskapGTAHPYDSGHIAMTYTGLSCLVILGDDLSRVNKEACLAGLRALQLEDGSFCAV--PEGSENDMRFVY 176
Cdd:cd02895 76 STLGLP-------GTASKYDTGNLAMTYFALLSLLILGDDLSRVDRKAILNFLSKLQLPDGSFGSVldSEGGENDMRFCY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 177 CASCICYMLNNWS--GMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEvFSEKELNRIKRWCIM 254
Cdd:cd02895 149 CAVAICYMLDDWSeeDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE-LSEKFLERLKRWLVH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 255 RQQN--GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02895 228 RQVSgtGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
|
|
| PLN03201 |
PLN03201 |
RAB geranylgeranyl transferase beta-subunit; Provisional |
14-355 |
8.10e-49 |
|
RAB geranylgeranyl transferase beta-subunit; Provisional
Pssm-ID: 215630 [Multi-domain] Cd Length: 316 Bit Score: 167.57 E-value: 8.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 14 EGERLDFLRDRHVRFFQRcLQVLPERYSSLETS--RLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQvlpteDRSnln 91
Cdd:PLN03201 2 SGPMGELVVDKHVRYIKS-LEKKKDSFESVVMEhlRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQ-----HES--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 92 rCGFRGSsylgipfnpskapgTAHpydSGHIAMTytgLSCLVILG--DDLSRVNKEACLAGLRALQLEDGSFcAVPEGSE 169
Cdd:PLN03201 73 -GGFGGN--------------TGH---DPHILYT---LSAVQILAlfDRLDLLDADKVASYVAGLQNEDGSF-SGDEWGE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 170 NDMRFVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsEKELnrIK 249
Cdd:PLN03201 131 IDTRFSYCALCCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHV--DKDL--LG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 250 RWCIMRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGIC 327
Cdd:PLN03201 207 WWLCERQvkSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVA 286
|
330 340
....*....|....*....|....*...
gi 767936130 328 GLSLMEESGICKVHPALNVSTRTSERLL 355
Cdd:PLN03201 287 GLSLLGYPGLKPIDPAYALPVDVVNRIG 314
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
112-333 |
2.23e-13 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 69.35 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 112 GTAHPYDSGHIAMTYTGLSCLVILGddLSRVNKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCAScICYMLNNWSGM 191
Cdd:COG5029 37 GFAGRSGPSDLYSTYYAVRTLALLG--ESPKWRDRVADLLSSLRVEDGGFAKAPEGGAGSTYHTYLAT-LLAELLGRPPP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 192 DMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEevfsEKELNRIKRWCIMRQQN--GYHGRPNKPV- 268
Cdd:COG5029 114 DPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD----DPIETKVIRFLRDVQSPegGFAYNTRIGEa 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767936130 269 DTCYSFWVGATLKLLKIfQYTNFEKNRNYILSTQdRLVGGFAKWP-DSHPDALHAYFGICGLSLME 333
Cdd:COG5029 190 DLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQ-LPDGGFEGAPwDGVEDVEYTFYGVGALALLG 253
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
191-234 |
1.78e-07 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 47.12 E-value: 1.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767936130 191 MDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMG 234
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| GGTase-I |
cd02895 |
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ... |
22-332 |
1.30e-172 |
|
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: 483.32 E-value: 1.30e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLD---VVNKDDIIEWIYSLQVLptedrSNLNRCGFRGS 98
Cdd:cd02895 1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDsilVEEKDDIIEWIYSLQVL-----SNLPRGGFRGS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 99 SYLGIPfnpskapGTAHPYDSGHIAMTYTGLSCLVILGDDLSRVNKEACLAGLRALQLEDGSFCAV--PEGSENDMRFVY 176
Cdd:cd02895 76 STLGLP-------GTASKYDTGNLAMTYFALLSLLILGDDLSRVDRKAILNFLSKLQLPDGSFGSVldSEGGENDMRFCY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 177 CASCICYMLNNWS--GMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEvFSEKELNRIKRWCIM 254
Cdd:cd02895 149 CAVAICYMLDDWSeeDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE-LSEKFLERLKRWLVH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 255 RQQN--GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02895 228 RQVSgtGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
|
|
| PTase |
cd02890 |
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ... |
22-332 |
7.45e-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: 381.55 E-value: 7.45e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDS-LDVVNKDDIIEWIYSLQVLPTedrsnlnrCGFRGSsy 100
Cdd:cd02890 1 REKHIKYLQRCLKLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNED--------GGFGGG-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 101 lgipfnpskapgtahPYDSGHIAMTYTGLSCLVILGDD-LSRVNKEACLAGLRALQLEDGSFCAVPEGsENDMRFVYCAS 179
Cdd:cd02890 71 ---------------PGQDPHLASTYAAVLSLAILGDDaLSRIDREKIYKFLSSLQNPDGSFRGDLGG-EVDTRFVYCAL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 180 CICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFsekeLNRIKRWCIMRQQN- 258
Cdd:cd02890 135 SILSLLNILTDIDKEKLIDYILSCQNYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLID----KERLLRWLVERQLAs 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767936130 259 --GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02890 211 ggGFNGRPNKLVDTCYSFWVGASLKILGRLHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
|
|
| ISOPREN_C2_like |
cd00688 |
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ... |
22-332 |
1.70e-60 |
|
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: 197.39 E-value: 1.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDML------DSLDVVNKDDIIEWIYSLQvlptedrsnLNRCGF 95
Cdd:cd00688 1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLlaatgiRDKADENIEKGIQRLLSYQ---------LSDGGF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 96 RGSSYlgipfnpskapgtahpYDSGHIAMTYTGLSCLVILGDD--LSRVNKEACLAGLRALQLEDGSFCAV------PEG 167
Cdd:cd00688 72 SGWGG----------------NDYPSLWLTAYALKALLLAGDYiaVDRIDLARALNWLLSLQNEDGGFREDgpgnhrIGG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 168 SENDMRFVYCASCICYMLNNWS-GMDMKKAITYIRRSMSYDNGLaqGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELn 246
Cdd:cd00688 136 DESDVRLTAYALIALALLGKLDpDPLIEKALDYLLSCQNYDGGF--GPGGESHGYGTACAAAALALLGDLDSPDAKKAL- 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 247 rikRWCIMRQQNGYHG-----RPNKPVDTCYSFWVGATLK-LLKIFQYTNFEKNRNYILStQDRLVGGFAKWPDSHPDAL 320
Cdd:cd00688 213 ---RWLLSRQRPDGGWgegrdRTNKLSDSCYTEWAAYALLaLGKLGDLEDAEKLVKWLLS-QQNEDGGFSSKPGKSYDTQ 288
|
330
....*....|..
gi 767936130 321 HAYFGICGLSLM 332
Cdd:cd00688 289 HTVFALLALSLY 300
|
|
| FTase |
cd02893 |
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ... |
22-331 |
1.55e-55 |
|
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: 184.36 E-value: 1.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVN-KDDIIEWIYSLQvlPTEDrsnlnrcGFRGSsy 100
Cdd:cd02893 1 REKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSyADDVISFLRRCQ--NPSG-------GFGGG-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 101 lgipfnpskapgtahPYDSGHIAMTYTGLSCLVILGDD--LSRVNKEACLAGLRALQLEDGSFcAVPEGSENDMRFVYCA 178
Cdd:cd02893 70 ---------------PGQLPHLATTYAAVNALAIIGTEeaYDVIDREALYKFLLSLKQPDGSF-RMHVGGEVDVRGTYCA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 179 SCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsekELNRIKRWCIMRQQN 258
Cdd:cd02893 134 ISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKL----DLESLLRWLVARQMR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 259 ---GYHGRPNKPVDTCYSFWVGATLKLLK-------------IFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHA 322
Cdd:cd02893 210 fegGFQGRTNKLVDGCYSFWVGGSLPILEailnaekkfddsaEGTLFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHT 289
|
....*....
gi 767936130 323 YFGICGLSL 331
Cdd:cd02893 290 CYALSGLSI 298
|
|
| GGTase-II |
cd02894 |
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ... |
20-332 |
1.71e-55 |
|
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: 184.01 E-value: 1.71e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 20 FLRDRHVRFFQrclQVLPERYSS----LETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQvlptedrsnLNRCGf 95
Cdd:cd02894 1 LLLEKHIEYIL---SLTKKKDDYeyilTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQ---------DNEDG- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 96 rgssylGIPFNPSkapgtahpYDSgHIAMTYTGLSCLvILGDDLSRV--NKEACLAGLRALQLEDGSFCAVPEGsENDMR 173
Cdd:cd02894 68 ------GFGGSPG--------HDP-HILSTLSAIQIL-ALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWG-EVDTR 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 174 FVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEkelnRIKRWCI 253
Cdd:cd02894 131 FSYCAVLCLTLLGKLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRD----RLGWWLC 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 254 MRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSL 331
Cdd:cd02894 207 ERQlpSGGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSL 286
|
.
gi 767936130 332 M 332
Cdd:cd02894 287 L 287
|
|
| PLN03201 |
PLN03201 |
RAB geranylgeranyl transferase beta-subunit; Provisional |
14-355 |
8.10e-49 |
|
RAB geranylgeranyl transferase beta-subunit; Provisional
Pssm-ID: 215630 [Multi-domain] Cd Length: 316 Bit Score: 167.57 E-value: 8.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 14 EGERLDFLRDRHVRFFQRcLQVLPERYSSLETS--RLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQvlpteDRSnln 91
Cdd:PLN03201 2 SGPMGELVVDKHVRYIKS-LEKKKDSFESVVMEhlRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQ-----HES--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 92 rCGFRGSsylgipfnpskapgTAHpydSGHIAMTytgLSCLVILG--DDLSRVNKEACLAGLRALQLEDGSFcAVPEGSE 169
Cdd:PLN03201 73 -GGFGGN--------------TGH---DPHILYT---LSAVQILAlfDRLDLLDADKVASYVAGLQNEDGSF-SGDEWGE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 170 NDMRFVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsEKELnrIK 249
Cdd:PLN03201 131 IDTRFSYCALCCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHV--DKDL--LG 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 250 RWCIMRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGIC 327
Cdd:PLN03201 207 WWLCERQvkSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVA 286
|
330 340
....*....|....*....|....*...
gi 767936130 328 GLSLMEESGICKVHPALNVSTRTSERLL 355
Cdd:PLN03201 287 GLSLLGYPGLKPIDPAYALPVDVVNRIG 314
|
|
| PLN02710 |
PLN02710 |
farnesyltranstransferase subunit beta |
17-284 |
1.42e-32 |
|
farnesyltranstransferase subunit beta
Pssm-ID: 215380 [Multi-domain] Cd Length: 439 Bit Score: 126.82 E-value: 1.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 17 RLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLD-SLDVVNKDDIIEWiyslqvlptedrsnLNRCGF 95
Cdd:PLN02710 41 MLELWREKHLEYLTRGLRQLGPSFSVLDANRPWLCYWILHSIALLGeSLDDELENDTIDF--------------LSRCQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 96 RGSSYLGipfNPSKAPgtahpydsgHIAMTYTGLSCLVILGDD--LSRVNKEACLAGLRALQLEDGSFcAVPEGSENDMR 173
Cdd:PLN02710 107 PNGGYGG---GPGQLP---------HLATTYAAVNTLVTIGGEraLSSINREKLYTFLLRMKDPSGGF-RMHDGGEMDVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 174 FVYCASCICYMLNNWSGMDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsekELNRIKRWCI 253
Cdd:PLN02710 174 ACYTAISVASLLNILDDELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRL----DLPSLINWVV 249
|
250 260 270
....*....|....*....|....*....|...
gi 767936130 254 MRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLK 284
Cdd:PLN02710 250 FRQgvEGGFQGRTNKLVDGCYSFWQGGVFALLQ 282
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
112-333 |
2.23e-13 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 69.35 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 112 GTAHPYDSGHIAMTYTGLSCLVILGddLSRVNKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCAScICYMLNNWSGM 191
Cdd:COG5029 37 GFAGRSGPSDLYSTYYAVRTLALLG--ESPKWRDRVADLLSSLRVEDGGFAKAPEGGAGSTYHTYLAT-LLAELLGRPPP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 192 DMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEevfsEKELNRIKRWCIMRQQN--GYHGRPNKPV- 268
Cdd:COG5029 114 DPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD----DPIETKVIRFLRDVQSPegGFAYNTRIGEa 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767936130 269 DTCYSFWVGATLKLLKIfQYTNFEKNRNYILSTQdRLVGGFAKWP-DSHPDALHAYFGICGLSLME 333
Cdd:COG5029 190 DLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQ-LPDGGFEGAPwDGVEDVEYTFYGVGALALLG 253
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
191-234 |
1.78e-07 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 47.12 E-value: 1.78e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767936130 191 MDMKKAITYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMG 234
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
290-333 |
5.56e-07 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 45.58 E-value: 5.56e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767936130 290 NFEKNRNYILSTQdRLVGGFAKWPDSHPDALHAYFGICGLSLME 333
Cdd:pfam00432 2 DKEKLVDYLLSCQ-NEDGGFGGRPGGESDTYYTYCALAALALLG 44
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
240-283 |
4.86e-06 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 43.27 E-value: 4.86e-06
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 767936130 240 FSEKELNRIKRWCiMRQQNGYHGRPNKPVDTCYSFWVGATLKLL 283
Cdd:pfam00432 1 IDKEKLVDYLLSC-QNEDGGFGGRPGGESDTYYTYCALAALALL 43
|
|
| CAL1 |
COG5029 |
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ... |
21-238 |
5.95e-06 |
|
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];
Pssm-ID: 444045 [Multi-domain] Cd Length: 259 Bit Score: 47.39 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 21 LRDRHVRFFQRCLQV---LPER--YSSLETSrltiaFFALSGLDMLdSLDVVNKDDIIEWIYSLQVlptEDRSNLNRCGF 95
Cdd:COG5029 20 FTDSHLDYLRASQNPdggFAGRsgPSDLYST-----YYAVRTLALL-GESPKWRDRVADLLSSLRV---EDGGFAKAPEG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 96 R-GSSY-----------LGIP----------------------FNPSKAPGTAhpydsghiaMTYTGLSCLVILGDdLSR 141
Cdd:COG5029 91 GaGSTYhtylatllaelLGRPppdpdrlvrflisqqnddggfeISPGRRSDTN---------PTAAAIGALRALGA-LDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 142 VNKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDmKKAITYIRrSMSYDNGLAQGAGLESHG- 220
Cdd:COG5029 161 PIETKVIRFLRDVQSPEGGFAYNTRIGEADLLSTFTAILTLYDLGAAPKLV-DDLQAYIL-SLQLPDGGFEGAPWDGVEd 238
|
250
....*....|....*....
gi 767936130 221 -GSTFCGIASLCLMGKLEE 238
Cdd:COG5029 239 vEYTFYGVGALALLGALAE 257
|
|
| Prenyltrans |
pfam00432 |
Prenyltransferase and squalene oxidase repeat; |
142-186 |
8.60e-06 |
|
Prenyltransferase and squalene oxidase repeat;
Pssm-ID: 395346 [Multi-domain] Cd Length: 44 Bit Score: 42.50 E-value: 8.60e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 767936130 142 VNKEACLAGLRALQLEDGSFCAVPEGsENDMRFVYCASCICYMLN 186
Cdd:pfam00432 1 IDKEKLVDYLLSCQNEDGGFGGRPGG-ESDTYYTYCALAALALLG 44
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
113-334 |
2.11e-04 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 42.40 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 113 TAHPYDSGHIAMTYTGLSCLVILGDDLSrvNKEACLAGLRALQLEDGSFCAVpegsendmrfvYCASCICYMLNnwsgmD 192
Cdd:COG1689 26 CAYPGLPSTLADTYYAVRILKLLGEEVP--NRDKTIEFLESCQDEEGGGFAL-----------YTTSYGLMALA-----L 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 193 MKKAITYIRRSMSY--DNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKrwciMRQQNGYHGRpnKPVDT 270
Cdd:COG1689 88 LGIDPPDEQEALEYlsDALPTKFAGGASDLEETYLAVALLEALGASEPEREKIREFLLS----LRRPDGGFGG--KKPNL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767936130 271 CYSFWVGATLKLLKIfQYTNFEKNRNYILSTQDRlVGGFAKWPDSHPDALHAYFGICGLSLMEE 334
Cdd:COG1689 162 EDTYWALAALRRLGR-DLPPADRVIAFILACQNE-DGGFSKTPGSYSDLEATYYALRALKLLGE 223
|
|
| AF1543 |
COG1689 |
Class II terpene cyclase family protein AF1543 [General function prediction only]; |
48-167 |
1.16e-03 |
|
Class II terpene cyclase family protein AF1543 [General function prediction only];
Pssm-ID: 441295 [Multi-domain] Cd Length: 272 Bit Score: 40.48 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767936130 48 LTIAFFALSGLDMLDSlDVVNKDDIIEWIYSLQvlpTEDRsnlnrcGFrgssylgipfnpSKAPGTaHPYdsghIAMTYT 127
Cdd:COG1689 161 LEDTYWALAALRRLGR-DLPPADRVIAFILACQ---NEDG------GF------------SKTPGS-YSD----LEATYY 213
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767936130 128 GLSCLVILGDDLSrvNKEACLAGLRALQLEDGSFCAVPEG 167
Cdd:COG1689 214 ALRALKLLGEPPK--NVDKLLEFIASCQNSDGGFRRSPEG 251
|
|
|