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Conserved domains on  [gi|15229948|ref|NP_187814|]
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RAB geranylgeranyl transferase beta subunit 2 [Arabidopsis thaliana]

Protein Classification

PLN03201 family protein( domain architecture ID 11477565)

PLN03201 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 1-316 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


:

Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 639.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    1 MADKLVAGKHLRYILNLmaEKKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQHESGGFAGNTGH 80
Cdd:PLN03201   4 PMGELVVDKHVRYIKSL--EKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   81 DPHVLYTLSAVQILALFDKLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYI 160
Cdd:PLN03201  82 DPHILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  161 VSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQdYESGGLNGRPEKLPDVCYSWWVLSSLI 240
Cdd:PLN03201 162 VSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQ-VKSGGLNGRPEKLPDVCYSWWVLSSLI 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229948  241 MIDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLLEYPGVKTIDPAYALPVHVINRILFT 316
Cdd:PLN03201 241 IIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
 
Name Accession Description Interval E-value
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 1-316 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 639.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    1 MADKLVAGKHLRYILNLmaEKKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQHESGGFAGNTGH 80
Cdd:PLN03201   4 PMGELVVDKHVRYIKSL--EKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   81 DPHVLYTLSAVQILALFDKLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYI 160
Cdd:PLN03201  82 DPHILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  161 VSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQdYESGGLNGRPEKLPDVCYSWWVLSSLI 240
Cdd:PLN03201 162 VSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQ-VKSGGLNGRPEKLPDVCYSWWVLSSLI 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229948  241 MIDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLLEYPGVKTIDPAYALPVHVINRILFT 316
Cdd:PLN03201 241 IIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 5-291 1.55e-175

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: 487.16  E-value: 1.55e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   5 LVAGKHLRYILNLmaEKKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQ-HESGGFAGNTGHDPH 83
Cdd:cd02894   1 LLLEKHIEYILSL--TKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  84 VLYTLSAVQILALFDKLNILD--VEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYIV 161
Cdd:cd02894  79 ILSTLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 162 SCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYeSGGLNGRPEKLPDVCYSWWVLSSLIM 241
Cdd:cd02894 159 SCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLP-SGGLNGRPEKLPDVCYSWWVLSSLKI 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15229948 242 IDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLL 291
Cdd:cd02894 238 IGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 58-292 1.95e-26

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 104.79  E-value: 1.95e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  58 DEVVSWVMTCQHESGGFAGNTGhDPHVLYTLSAVQILALFDKLNILDvEKVSNYIAGLQNEDGSF-------SGDIWGev 130
Cdd:COG5029  22 DSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFakapeggAGSTYH-- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 131 dtrfSYIAICCLSILKcLDKINVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCE 210
Cdd:COG5029  98 ----TYLATLLAELLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRD 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 211 RQDYESGGLNGRPEKLPDVCYSWWVLSSLIMIDrVHWIEKAKLVKFILDSQdMDNGGISDRPSYTV-DIFHTYFGVAGLS 289
Cdd:COG5029 173 VQSPEGGFAYNTRIGEADLLSTFTAILTLYDLG-AAPKLVDDLQAYILSLQ-LPDGGFEGAPWDGVeDVEYTFYGVGALA 250


                ...
gi 15229948 290 LLE 292
Cdd:COG5029 251 LLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
151-194 1.23e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 61.37  E-value: 1.23e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15229948   151 INVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALAITG 194
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 61-171 1.33e-06

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: 49.75  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    61 VSWVMTCQHESGGFAG----NTGH-----DPHVLY------------TLSAVQILALFdKLNILDVEKVSN----YIAGL 115
Cdd:TIGR01787 394 VNWILGMQSSNGGFAAydpdNTGEwlellNPSEVFgdimidppyvdvTARVIQALGAF-GHRADEIRNVLEraleYLRRE 472

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229948   116 QNEDGSFSGDiWGevdTRFSYIAICCLSILKCLDKI-----NVKKAVDYIVSCKNLDGGFG 171
Cdd:TIGR01787 473 QRADGSWFGR-WG---VNYTYGTGFVLSALAAAGRTyrncpEVQKACDWLLSRQMPDGGWG 529
 
Name Accession Description Interval E-value
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 1-316 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 639.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    1 MADKLVAGKHLRYILNLmaEKKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQHESGGFAGNTGH 80
Cdd:PLN03201   4 PMGELVVDKHVRYIKSL--EKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGH 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   81 DPHVLYTLSAVQILALFDKLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYI 160
Cdd:PLN03201  82 DPHILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  161 VSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQdYESGGLNGRPEKLPDVCYSWWVLSSLI 240
Cdd:PLN03201 162 VSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQ-VKSGGLNGRPEKLPDVCYSWWVLSSLI 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15229948  241 MIDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLLEYPGVKTIDPAYALPVHVINRILFT 316
Cdd:PLN03201 241 IIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 5-291 1.55e-175

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: 487.16  E-value: 1.55e-175
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   5 LVAGKHLRYILNLmaEKKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQ-HESGGFAGNTGHDPH 83
Cdd:cd02894   1 LLLEKHIEYILSL--TKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPH 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  84 VLYTLSAVQILALFDKLNILD--VEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYIV 161
Cdd:cd02894  79 ILSTLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 162 SCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYeSGGLNGRPEKLPDVCYSWWVLSSLIM 241
Cdd:cd02894 159 SCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLP-SGGLNGRPEKLPDVCYSWWVLSSLKI 237

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 15229948 242 IDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLL 291
Cdd:cd02894 238 IGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 9-291 9.42e-142

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: 401.58  E-value: 9.42e-142
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   9 KHLRYILNLMaekKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSE-DEVVSWVMTCQ-HESGGFAGNTGHDPHVLY 86
Cdd:cd02890   3 KHIKYLQRCL---KLLPSSYTSLDASRLWLLYWILSSLDLLGEDLDDENkDEIIDFIYSCQvNEDGGFGGGPGQDPHLAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  87 TLSAVQILALFDK--LNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYIVSCK 164
Cdd:cd02890  80 TYAAVLSLAILGDdaLSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 165 NLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYESGGLNGRPEKLPDVCYSWWVLSSLIMIDR 244
Cdd:cd02890 160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGGGFNGRPNKLVDTCYSFWVGASLKILGR 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15229948 245 VHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLL 291
Cdd:cd02890 240 LHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 9-291 1.38e-72

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: 226.28  E-value: 1.38e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   9 KHLRYILNLMaekKKESFESVVMDHLRMNGAYWGLTTLALLDKLGSVSE------DEVVSWVMTCQHESGGFAGNTGHD- 81
Cdd:cd00688   3 KHLKYLLRYP---YGDGHWYQSLCGEQTWSTAWPLLALLLLLAATGIRDkadeniEKGIQRLLSYQLSDGGFSGWGGNDy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  82 PHVLYTLSAVQILALFDKLNILD---VEKVSNYIAGLQNEDGSFSGDIWG-------EVDTRFSYIAICCLSILKCL-DK 150
Cdd:cd00688  80 PSLWLTAYALKALLLAGDYIAVDridLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLdPD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 151 INVKKAVDYIVSCKNLDGGFGcsPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYESGGLNGR--PEKLPD 228
Cdd:cd00688 160 PLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRdrTNKLSD 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229948 229 VCYSWWVLSSLIMIDRV-HWIEKAKLVKFILdSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLL 291
Cdd:cd00688 238 SCYTEWAAYALLALGKLgDLEDAEKLVKWLL-SQQNEDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 9-291 2.79e-68

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: 215.22  E-value: 2.79e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   9 KHLRYI---LNLMAEkkkeSFESVvmDHLRMNGAYWGLTTLALLDKLGSVSEDE---VVSWVMTCQ----HESGGFAGNT 78
Cdd:cd02895   3 KHVKFFqrcLQLLPS----SYQSL--DTNRLTIAFFALSGLDLLGALDSILVEEkddIIEWIYSLQvlsnLPRGGFRGSS 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  79 GHD----------PHVLYTLSAVQILA-LFDKLNILDVEKVSNYIAGLQNEDGSFSGDIW---GEVDTRFSYIAICCLSI 144
Cdd:cd02895  77 TLGlpgtaskydtGNLAMTYFALLSLLiLGDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYM 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 145 LKCLDK--INVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVD---KDLLGWWLCERQdYESGGL 219
Cdd:cd02895 157 LDDWSEedIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEELSekfLERLKRWLVHRQ-VSGTGF 235

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15229948 220 NGRPEKLPDVCYSWWVLSSLIMIDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLL 291
Cdd:cd02895 236 NGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 9-290 2.64e-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: 204.78  E-value: 2.64e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   9 KHLRYiLNLMAEKKKESFESVvmDHLRMNGAYWGLTTLALLDKLGSVS-EDEVVSWVMTCQHESGGFAGNTGHDPHVLYT 87
Cdd:cd02893   3 KHIKY-LKKSLRQLPSSFTSL--DASRPWLLYWILHSLELLGEELDQSyADDVISFLRRCQNPSGGFGGGPGQLPHLATT 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  88 LSAVQILALFD---KLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYIVSCK 164
Cdd:cd02893  80 YAAVNALAIIGteeAYDVIDREALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 165 NLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYESGGLNGRPEKLPDVCYSWWVLSSLIMIDR 244
Cdd:cd02893 160 TYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLRWLVARQMRFEGGFQGRTNKLVDGCYSFWVGGSLPILEA 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15229948 245 V------------HW-IEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSL 290
Cdd:cd02893 240 IlnaekkfddsaeGTlFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 9-310 1.92e-36

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 135.68  E-value: 1.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    9 KHLRYILNLMaEKKKESFEsvVMDHLRMNGAYWGLTTLALLDK-LGSVSEDEVVSWVMTCQHESGGFAGNTGHDPHVLYT 87
Cdd:PLN02710  48 KHLEYLTRGL-RQLGPSFS--VLDANRPWLCYWILHSIALLGEsLDDELENDTIDFLSRCQDPNGGYGGGPGQLPHLATT 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   88 LSAVQILALF---DKLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSILKCLDKINVKKAVDYIVSCK 164
Cdd:PLN02710 125 YAAVNTLVTIggeRALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQ 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  165 NLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDYEsGGLNGRPEKLPDVCYSWWVLSSLIMIDR 244
Cdd:PLN02710 205 TYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVE-GGFQGRTNKLVDGCYSFWQGGVFALLQQ 283

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  245 VHWIEKAKLV-----------------------------------------------------------KFILDSQDMDN 265
Cdd:PLN02710 284 LVTIVDEQLQtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnqqmgplfhsialqQYILLCSQVLD 363

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 15229948  266 GGISDRPSYTVDIFHTYFGVAGLSLLEYPGVKTIDpAYALPVHVI 310
Cdd:PLN02710 364 GGLRDKPGKSRDYYHTCYCLSGLSVAQYSASKDED-SPPLPRHVL 407
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 58-292 1.95e-26

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 104.79  E-value: 1.95e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  58 DEVVSWVMTCQHESGGFAGNTGhDPHVLYTLSAVQILALFDKLNILDvEKVSNYIAGLQNEDGSF-------SGDIWGev 130
Cdd:COG5029  22 DSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFakapeggAGSTYH-- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 131 dtrfSYIAICCLSILKcLDKINVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCE 210
Cdd:COG5029  98 ----TYLATLLAELLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRD 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 211 RQDYESGGLNGRPEKLPDVCYSWWVLSSLIMIDrVHWIEKAKLVKFILDSQdMDNGGISDRPSYTV-DIFHTYFGVAGLS 289
Cdd:COG5029 173 VQSPEGGFAYNTRIGEADLLSTFTAILTLYDLG-AAPKLVDDLQAYILSLQ-LPDGGFEGAPWDGVeDVEYTFYGVGALA 250


                ...
gi 15229948 290 LLE 292
Cdd:COG5029 251 LLG 253
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
58-292 1.08e-14

Class II terpene cyclase family protein AF1543 [General function prediction only];


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 72.83  E-value: 1.08e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  58 DEVVSWVMTCQHESGGFAGNTGHDPHVLYTLSAVQILALFDKlNILDVEKVSNYIAGLQNEDGSFSGdiwgevdTRFSYI 137
Cdd:COG1689   9 ARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLGE-EVPNRDKTIEFLESCQDEEGGGFA-------LYTTSY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 138 AICCLSILKCLD-----------------------------------------KINVKKAVDYIVSCKNLDGGFGCSPGa 176
Cdd:COG1689  81 GLMALALLGIDPpdeqealeylsdalptkfaggasdleetylavallealgasEPEREKIREFLLSLRRPDGGFGGKKP- 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 177 esHAGQIFCCVGALAITGNLHRVDKDLLGWWL-CERQDyesGGLNGRPEKLPDVCYSWWVLSSLIMIDrvhwiEKAKLVK 255
Cdd:COG1689 160 --NLEDTYWALAALRRLGRDLPPADRVIAFILaCQNED---GGFSKTPGSYSDLEATYYALRALKLLG-----EPPKNVD 229

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15229948 256 ----FILDSQdMDNGGISDRPSYTV-DIFHTYFGVAGLSLLE 292
Cdd:COG1689 230 klleFIASCQ-NSDGGFRRSPEGGIsTLEYTYYALAVLKWLK 270
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
57-198 1.28e-14

Class II terpene cyclase family protein AF1543 [General function prediction only];


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 72.45  E-value: 1.28e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  57 EDEVVSWVMTCQHESGGFAGNtghDPHVLYTLSAVQILALFDKLnILDVEKVSNYIAGLQNEDGSFS---GDIWGEVDTr 133
Cdd:COG1689 137 REKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRLGRD-LPPADRVIAFILACQNEDGGFSktpGSYSDLEAT- 211

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15229948 134 fsYIAICCLSILKcLDKINVKKAVDYIVSCKNLDGGFGCSPgaESHAGQIFCCVGALAITGNLHR 198
Cdd:COG1689 212 --YYALRALKLLG-EPPKNVDKLLEFIASCQNSDGGFRRSP--EGGISTLEYTYYALAVLKWLKR 271
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
151-194 1.23e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 61.37  E-value: 1.23e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 15229948   151 INVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALAITG 194
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 40-194 3.00e-11

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 62.80  E-value: 3.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  40 YWGLTTLALLDKlgSV-SEDEVVSWVMTCQHESGGFAGNTGHDPHVLYTLSAVQILALFDKLNILDVEKVSNYIAGLQNE 118
Cdd:COG5029  99 YLATLLAELLGR--PPpDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSP 176

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229948 119 DGSFS-GDIWGEVDTRFSYIAICCLSILKCLDKInVKKAVDYIVSCKNLDGGFGCSPGAES-HAGQIFCCVGALAITG 194
Cdd:COG5029 177 EGGFAyNTRIGEADLLSTFTAILTLYDLGAAPKL-VDDLQAYILSLQLPDGGFEGAPWDGVeDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
104-145 8.35e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 56.37  E-value: 8.35e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15229948   104 DVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAICCLSIL 145
Cdd:pfam00432   2 DKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALL 43
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 158-293 1.22e-10

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 60.88  E-value: 1.22e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 158 DYIVSCKNLDGGFGCSPGaESHAGQIFCCVGALAITGNLHRVDKDLLGWWL-CERQDyesGGLNGRPEKLPDVCY-SWWV 235
Cdd:COG5029  26 DYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRVED---GGFAKAPEGGAGSTYhTYLA 101

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15229948 236 LSSLIMIDRVHWIEKAkLVKFILDSQDmDNGGISDRPSYTVDIFHTYFGVAGLSLLEY 293
Cdd:COG5029 102 TLLAELLGRPPPDPDR-LVRFLISQQN-DDGGFEISPGRRSDTNPTAAAIGALRALGA 157
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
99-294 5.15e-10

Class II terpene cyclase family protein AF1543 [General function prediction only];


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 58.97  E-value: 5.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  99 KLNILDVEKVSNYIAGLQNEDGSFSGDIWGEVDTRFSYIAIcclSILKCLDKI--NVKKAVDYIVSCKNLDGG------- 169
Cdd:COG1689   2 TSLRFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAV---RILKLLGEEvpNRDKTIEFLESCQDEEGGgfalytt 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 170 -FGCS---------------------------PGAESHAGQIFCCVGALAITGNLHRVDKDLLGWWLCERQDyeSGGLNG 221
Cdd:COG1689  79 sYGLMalallgidppdeqealeylsdalptkfAGGASDLEETYLAVALLEALGASEPEREKIREFLLSLRRP--DGGFGG 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15229948 222 rpeKLPDVCYSWWVLSSLIMIDRvHWIEKAKLVKFILDSQDMDnGGISDRPSYTVDIFHTYFGVAGLSLLEYP 294
Cdd:COG1689 157 ---KKPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQNED-GGFSKTPGSYSDLEATYYALRALKLLGEP 224
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
199-243 1.74e-09

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 52.51  E-value: 1.74e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15229948   199 VDKDLLGWWLCERQDyESGGLNGRPEKLPDVCYSWWVLSSLIMID 243
Cdd:pfam00432   1 IDKEKLVDYLLSCQN-EDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
57-98 1.18e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 50.20  E-value: 1.18e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15229948    57 EDEVVSWVMTCQHESGGFAGNTGHDPHVLYTLSAVQILALFD 98
Cdd:pfam00432   3 KEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
37-239 2.48e-08

Class II terpene cyclase family protein AF1543 [General function prediction only];


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 53.96  E-value: 2.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  37 NGAYWGLTTLALLDKLgSVSEDEVVSWvMTCQHESGGFAGNTghdphvlyTLSAVQIL-ALFDKLNIL--DVEKVSNYIA 113
Cdd:COG1689  76 YTTSYGLMALALLGID-PPDEQEALEY-LSDALPTKFAGGAS--------DLEETYLAvALLEALGASepEREKIREFLL 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 114 GLQNEDGSFSGDIWGEVDTRFsyiaicCLSILKCLDK--INVKKAVDYIVSCKNLDGGFGCSPGAESHAGQIFCCVGALA 191
Cdd:COG1689 146 SLRRPDGGFGGKKPNLEDTYW------ALAALRRLGRdlPPADRVIAFILACQNEDGGFSKTPGSYSDLEATYYALRALK 219

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15229948 192 ITGNLHRVDKDLLGWWL-CERQDyesGGLNGRPEK-LPDVCYSWWVLSSL 239
Cdd:COG1689 220 LLGEPPKNVDKLLEFIAsCQNSD---GGFRRSPEGgISTLEYTYYALAVL 266
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 26-146 1.74e-07

Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, Lipid transport and metabolism];


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 51.63  E-value: 1.74e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  26 FESVVMDHLRMNGAYWGLTTLALLDKLGSVSEDEVVSWVMTCQHESGGFAGNTGH-DPHVLYTLSAVQILalfDKLNI-- 102
Cdd:COG5029 132 FEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYNTRIgEADLLSTFTAILTL---YDLGAap 208

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15229948 103 LDVEKVSNYIAGLQNEDGSFSGDIWGEV-DTRFSYIAICCLSILK 146
Cdd:COG5029 209 KLVDDLQAYILSLQLPDGGFEGAPWDGVeDVEYTFYGVGALALLG 253
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 42-305 5.08e-07

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: 50.68  E-value: 5.08e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  42 GLTTLALLDKLGSVSE-------DEVVSWVMTCQHESGGFA----GNTG----------HD-----PHVLYTLSAVQILA 95
Cdd:cd02889  97 ALKALLRLQKKPPDGKkvsrerlYDAVDWLLSMQNSNGGFAafepDNTYkylelipevdGDimidpPYVECTGSVLEALG 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  96 LFDKLNILDVEKVSN-------YIAGLQNEDGSFSGDiWGevdTRFSYIAICCLSILKCLDKIN----VKKAVDYIVSCK 164
Cdd:cd02889 177 LFGKLYPEHRREIDPairravkYLEREQEPDGSWYGR-WG---VCFIYGTWFALEALAAAGEDEnspyVRKACDWLLSKQ 252

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948 165 NLDGGFGcspgaESHAGqifccvgalaitgnlhrvdkdllgwwlCERQDYESGGlngrpekLPDVCYSWWVLSSLIMIDR 244
Cdd:cd02889 253 NPDGGWG-----ESYES---------------------------YEDPSYAGGG-------RSTVVQTAWALLALMAAGE 293

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229948 245 VHWIEKAKLVKFILDSQDMDngGISDRPSYTvDIFHTYFGvaglslLEYPGVKTIDPAYAL 305
Cdd:cd02889 294 PDSEAVKRGVKYLLNTQQED--GDWPQEEIT-GVFFKNFY------IRYHNYRNYFPLWAL 345
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 61-171 1.33e-06

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: 49.75  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    61 VSWVMTCQHESGGFAG----NTGH-----DPHVLY------------TLSAVQILALFdKLNILDVEKVSN----YIAGL 115
Cdd:TIGR01787 394 VNWILGMQSSNGGFAAydpdNTGEwlellNPSEVFgdimidppyvdvTARVIQALGAF-GHRADEIRNVLEraleYLRRE 472

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15229948   116 QNEDGSFSGDiWGevdTRFSYIAICCLSILKCLDKI-----NVKKAVDYIVSCKNLDGGFG 171
Cdd:TIGR01787 473 QRADGSWFGR-WG---VNYTYGTGFVLSALAAAGRTyrncpEVQKACDWLLSRQMPDGGWG 529
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
248-292 5.98e-06

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 42.50  E-value: 5.98e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 15229948   248 IEKAKLVKFILDSQdMDNGGISDRPSYTVDIFHTYFGVAGLSLLE 292
Cdd:pfam00432   1 IDKEKLVDYLLSCQ-NEDGGFGGRPGGESDTYYTYCALAALALLG 44
SQCY_1 cd02892
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
 61-171 7.59e-05

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: 44.11  E-value: 7.59e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948  61 VSWVMTCQHESGGFAG----NTGHD-----------------PHVLYTLSAVQILALFDKLN---ILDVEKVSN----YI 112
Cdd:cd02892 406 VDWLLGMQNSNGGFAAfepdNTYHWlenlnpfedfgdimidpPYVECTGSVLEALGLFGKLYpghRREIDPAIRravkYL 485

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15229948 113 AGLQNEDGSFSGDiWGevdTRFSYIAICCLSILKC--LDKIN---VKKAVDYIVSCKNLDGGFG 171
Cdd:cd02892 486 LREQEPDGSWYGR-WG---VCYIYGTWFALEALAAagEDYENspyIRKACDFLLSKQNPDGGWG 545
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 234-300 8.63e-04

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: 40.26  E-value: 8.63e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15229948 234 WVLSSLIMIDR-VHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLLEYPGVKTID 300
Cdd:cd02890  32 WILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSLAILGDDALSRID 99
PLN02993 PLN02993
lupeol synthase
 87-173 1.15e-03

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 40.67  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   87 TLSAVQILALFDKLN--------ILDVEKVSNYIAGLQNEDGSFSGDiWGEVDTRFSYIAICCLSIL-----KCLdkiNV 153
Cdd:PLN02993 566 TSAVIQALVLFKQLYpdhrtkeiIKSIEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAgktynDCL---AM 641

                         90       100
                 ....*....|....*....|
gi 15229948  154 KKAVDYIVSCKNLDGGFGCS 173
Cdd:PLN02993 642 RKGVHFLLTIQRDDGGWGES 661
squa_tetra_cyc TIGR04277
squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, ...
 58-171 1.57e-03

squalene--tetrahymanol cyclase; This enzyme, also called squalene--tetrahymanol cyclase, occurs a small number of eukaryotes, some of them anaerobic. The pathway can occur under anaerobic conditions, and the product is thought to replace sterols, letting organisms with this compound build membrane suitable for performing phagocytosis.


Pssm-ID: 212000 [Multi-domain]  Cd Length: 624  Bit Score: 40.00  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948    58 DEVVSWVMTCQHESGGF----AGNTGHDPhvLYTLsAVQILALFDKLNILD-------------------------VEKV 108
Cdd:TIGR04277 386 DEGAEFLFSMQNDDGGFpafdKGKMEDNL--LFKF-AFKIAGIADSAEIFDpscpditahileglgefgdqanhdqIQKM 462

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15229948   109 SNYIAGLQNEDGSFSGDiWGevdtrFSYIaICCLSILKCLDKIN-------VKKAVDYIVSCKNLDGGFG 171
Cdd:TIGR04277 463 IKYFMDTQEKFGSWEAR-WG-----INYI-MAAGAVLPALAKMNydlnegwAKNAINWLLNKQNADGGFG 525
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 234-292 5.49e-03

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: 38.02  E-value: 5.49e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15229948 234 WVLSSLIMIDRVHWIEKAKLVKFILDSQDMDNGGISDRPSYTVDIFHTYFGVAGLSLLE 292
Cdd:cd02894  35 WGLTALDLLGQLERLNREEIIEFVKSCQDNEDGGFGGSPGHDPHILSTLSAIQILALYD 93
 
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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