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Conserved domains on  [gi|254553295|ref|NP_001156951|]
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geranylgeranyl transferase type-2 subunit beta isoform 3 [Mus musculus]

Protein Classification

geranylgeranyl transferase type-2 subunit beta( domain architecture ID 10121021)

geranylgeranyl transferase type-2 subunit beta is part of the catalytic component of the enzyme that catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX, such as RAB1A, RAB3A, RAB5A and RAB7A

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 1-261 0e+00

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: 508.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   1 MSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQ-HECGGISASIGHDPHLLYTLSAVQILTLYDSVHVI--NVD 77
Cdd:cd02894   24 LTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHILSTLSAIQILALYDLLNKIdeNKE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  78 KVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCC 157
Cdd:cd02894  104 KIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCC 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 158 TGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGG 237
Cdd:cd02894  184 VGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGG 263

                        250       260
                 ....*....|....*....|....
gi 254553295 238 FADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:cd02894  264 FADRPGNMVDVFHTFFGLAGLSLL 287
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 1-261 0e+00

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: 508.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   1 MSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQ-HECGGISASIGHDPHLLYTLSAVQILTLYDSVHVI--NVD 77
Cdd:cd02894   24 LTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHILSTLSAIQILALYDLLNKIdeNKE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  78 KVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCC 157
Cdd:cd02894  104 KIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCC 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 158 TGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGG 237
Cdd:cd02894  184 VGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGG 263

                        250       260
                 ....*....|....*....|....
gi 254553295 238 FADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:cd02894  264 FADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 3-283 5.33e-175

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 485.74  E-value: 5.33e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   3 EYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSVHVINVDKVVAY 82
Cdd:PLN03201  33 EHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDPHILYTLSAVQILALFDRLDLLDADKVASY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  83 VQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLA 162
Cdd:PLN03201 113 VAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 163 ITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRP 242
Cdd:PLN03201 193 ITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRP 272

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 254553295 243 GDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRV 283
Cdd:PLN03201 273 DDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 28-262 7.24e-29

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 110.95  E-value: 7.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  28 REEILVFIKSCQHECGGISASIGhDPHLLYTLSAVQILTLYDSVHVINvDKVVAYVQSLQKEDGSFA-------GDIWGe 100
Cdd:COG5029   21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 101 idtrfSFCAVATLALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLC 180
Cdd:COG5029   98 -----TYLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 181 ERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGL 258
Cdd:COG5029  172 DVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGAL 249


                 ....
gi 254553295 259 SLLG 262
Cdd:COG5029  250 ALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
122-163 1.93e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.60  E-value: 1.93e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 254553295  122 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 163
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 75-142 2.31e-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: 42.43  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   75 NVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKAIEFVLSCMNFDGGFG 142
Cdd:TIGR01787 461 VLERALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWLLSRQMPDGGWG 529
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 1-261 0e+00

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: 508.35  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   1 MSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQ-HECGGISASIGHDPHLLYTLSAVQILTLYDSVHVI--NVD 77
Cdd:cd02894   24 LTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHILSTLSAIQILALYDLLNKIdeNKE 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  78 KVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCC 157
Cdd:cd02894  104 KIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCC 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 158 TGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGG 237
Cdd:cd02894  184 VGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGG 263

                        250       260
                 ....*....|....*....|....
gi 254553295 238 FADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:cd02894  264 FADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 3-283 5.33e-175

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 485.74  E-value: 5.33e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   3 EYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDSVHVINVDKVVAY 82
Cdd:PLN03201  33 EHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDPHILYTLSAVQILALFDRLDLLDADKVASY 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  83 VQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLA 162
Cdd:PLN03201 113 VAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 163 ITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEETGGFADRP 242
Cdd:PLN03201 193 ITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRP 272

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 254553295 243 GDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRV 283
Cdd:PLN03201 273 DDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 1-261 1.97e-143

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: 404.66  E-value: 1.97e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   1 MSEYLRMSGVYWGLTVMDLMGQ-LHRMNREEILVFIKSCQ-HECGGISASIGHDPHLLYTLSAVQILTLYDS--VHVINV 76
Cdd:cd02890   21 SLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHLASTYAAVLSLAILGDdaLSRIDR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  77 DKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYC 156
Cdd:cd02890  101 EKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQNYDGGFGGVPGAESHGGYTFC 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 157 CTGFLAITSQLHQVNSDLLGWWLCERQLPSG-GLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREKLRSFILACQDEET 235
Cdd:cd02890  181 AVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKILGRLHLIDQEKLREYILSCQQSEV 260

                        250       260
                 ....*....|....*....|....*.
gi 254553295 236 GGFADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:cd02890  261 GGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 1-261 3.88e-74

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: 229.36  E-value: 3.88e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   1 MSEYLRMSGVYWGLTVMDLMGQLH------RMNREEILVFIKSCQHECGGISASIGHD-PHLLYTLSAVQILTL---YDS 70
Cdd:cd00688   21 SLCGEQTWSTAWPLLALLLLLAATgirdkaDENIEKGIQRLLSYQLSDGGFSGWGGNDyPSLWLTAYALKALLLagdYIA 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  71 VHVINVDKVVAYVQSLQKEDGSFAGDIWG-------EIDTRFSFCAVATLALLGKLDA-INVEKAIEFVLSCMNFDGGFG 142
Cdd:cd00688  101 VDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDPdPLIEKALDYLLSCQNYDGGFG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 143 crPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPE---KLPDVCYSWWVLASLKIIGRL-HWI 218
Cdd:cd00688  181 --PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnKLSDSCYTEWAAYALLALGKLgDLE 258

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 254553295 219 DREKLRSFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:cd00688  259 DAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 6-261 1.23e-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: 217.92  E-value: 1.23e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   6 RMSGVYWGLTVMDLMGQLHRM---NREEILVFIKSCQ----HECGGISASIGHD----------PHLLYTLSAVQIL-TL 67
Cdd:cd02895   26 RLTIAFFALSGLDLLGALDSIlveEKDDIIEWIYSLQvlsnLPRGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLlIL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  68 YDSVHVINVDKVVAYVQSLQKEDGSFAGDIW---GEIDTRFSFCAVATLALLG--KLDAINVEKAIEFVLSCMNFDGGFG 142
Cdd:cd02895  106 GDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYMLDdwSEEDIDKEKLIDYIKSSQSYDGGFG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 143 CRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGW---WLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWID 219
Cdd:cd02895  186 QGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERlkrWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLID 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 254553295 220 REKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:cd02895  266 FEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 10-260 3.94e-65

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: 205.93  E-value: 3.94e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  10 VYWGLTVMDLMG-QLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTL---YDSVHVINVDKVVAYVQS 85
Cdd:cd02893   30 LYWILHSLELLGeELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTYAAVNALAIigtEEAYDVIDREALYKFLLS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  86 LQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITS 165
Cdd:cd02893  110 LKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 166 QLHQVNSDLLGWWLCERQLPS-GGLNGRPEKLPDVCYSWWVLASLKIIGRL------------HW-IDREKLRSFILACQ 231
Cdd:cd02893  190 KPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPILEAIlnaekkfddsaeGTlFDQEALQEYILLCC 269

                        250       260
                 ....*....|....*....|....*....
gi 254553295 232 DEETGGFADRPGDMVDPFHTLFGIAGLSL 260
Cdd:cd02893  270 QSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 11-259 2.82e-30

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 117.96  E-value: 2.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  11 YWGLTVMDLMGQLHRMNRE-EILVFIKSCQHECGGISASIGHDPHLLYTLSAVQIL-TL--YDSVHVINVDKVVAYVQSL 86
Cdd:PLN02710  76 YWILHSIALLGESLDDELEnDTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLvTIggERALSSINREKLYTFLLRM 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  87 QKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQ 166
Cdd:PLN02710 156 KDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINE 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 167 LHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWIDREK------------------------ 222
Cdd:PLN02710 236 VDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFALLQQLVTIVDEQlqtggssimfeeleddacetsssg 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254553295 223 -----------------------------------LRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLS 259
Cdd:PLN02710 316 kddagdtdsadyskvgfdfikasnqqmgplfhsiaLQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLS 387
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 28-262 7.24e-29

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 110.95  E-value: 7.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  28 REEILVFIKSCQHECGGISASIGhDPHLLYTLSAVQILTLYDSVHVINvDKVVAYVQSLQKEDGSFA-------GDIWGe 100
Cdd:COG5029   21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 101 idtrfSFCAVATLALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLC 180
Cdd:COG5029   98 -----TYLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 181 ERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGL 258
Cdd:COG5029  172 DVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGAL 249


                 ....
gi 254553295 259 SLLG 262
Cdd:COG5029  250 ALLG 253
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
25-264 7.72e-21

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 89.40  E-value: 7.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  25 RMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDsVHVINVDKVVAYVQSLQKEDGSFAGdiwgeidTR 104
Cdd:COG1689    5 RFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLG-EEVPNRDKTIEFLESCQDEEGGGFA-------LY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 105 FSFCAVATLALLGKLDAINVEkAIEFvLSCMNFDGgfgcRPGSESHAGQIYCCT-GFLAitsqLHQVNSDLLGW--WLCE 181
Cdd:COG1689   77 TTSYGLMALALLGIDPPDEQE-ALEY-LSDALPTK----FAGGASDLEETYLAVaLLEA----LGASEPEREKIreFLLS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 182 RQLPSGGLNGrpeKLPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 261
Cdd:COG1689  147 LRRPDGGFGG---KKPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQN-EDGGFSKTPGSYSDLEATYYALRALKLL 221


                 ...
gi 254553295 262 GEE 264
Cdd:COG1689  222 GEP 224
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 11-215 1.21e-20

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 88.61  E-value: 1.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  11 YWGLTVMDLMGQLHRmNREEILVFIKSCQHECGG-------ISASIGHdpHLLYTLSAVqiltLYDsVHVINVDKVVAYV 83
Cdd:COG5029   51 YYAVRTLALLGESPK-WRDRVADLLSSLRVEDGGfakapegGAGSTYH--TYLATLLAE----LLG-RPPPDPDRLVRFL 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  84 QSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPgSESHAGQIYCCTGfLAI 163
Cdd:COG5029  123 ISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYNT-RIGEADLLSTFTA-ILT 200

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 254553295 164 TSQLHQVNSDL--LGWWLCERQLPSGGLNGRP-EKLPDVCYSWWVLASLKIIGRL 215
Cdd:COG5029  201 LYDLGAAPKLVddLQAYILSLQLPDGGFEGAPwDGVEDVEYTFYGVGALALLGAL 255
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
10-145 1.17e-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: 1.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  10 VYWGLTVMDLMGQLHRMnREEILVFIKSCQHECGGISASighDPHLLYTLSAVQILTLYDsVHVINVDKVVAYVQSLQKE 89
Cdd:COG1689  120 TYLAVALLEALGASEPE-REKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRLG-RDLPPADRVIAFILACQNE 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254553295  90 DGSFA---GDIWgeiDTRFSFCAVATLALLGKlDAINVEKAIEFVLSCMNFDGGFGCRP 145
Cdd:COG1689  195 DGGFSktpGSYS---DLEATYYALRALKLLGE-PPKNVDKLLEFIASCQNSDGGFRRSP 249
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
122-163 1.93e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.60  E-value: 1.93e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 254553295  122 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 163
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
74-215 1.37e-11

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 63.59  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  74 INVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFsfcAVATLALLGKlDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQ 153
Cdd:COG1689  135 PEREKIREFLLSLRRPDGGFGGKKPNLEDTYW---ALAALRRLGR-DLPPADRVIAFILACQNEDGGFSKTPGSYSDLEA 210

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254553295 154 IYCCTGFLAITSQLHQVNSDLLgWWLCERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRL 215
Cdd:COG1689  211 TYYALRALKLLGEPPKNVDKLL-EFIASCQNSDGGFRRSPEGgISTLEYTYYALAVLKWLKRL 272
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
74-117 3.68e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.14  E-value: 3.68e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 254553295   74 INVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLG 117
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
170-213 4.41e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 56.75  E-value: 4.41e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 254553295  170 VNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 213
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
218-262 7.81e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 55.98  E-value: 7.81e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 254553295  218 IDREKLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLG 262
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 118-263 1.03e-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: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 118 KLDAINVEKAIEFVLSCMNFDGGFGCRPGsESHAGQIYCCTGFLAITSQLHQVNSDLLGWWL-CERqlPSGGLNGRPEKL 196
Cdd:COG5029   15 KSTADFTDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRV--EDGGFAKAPEGG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254553295 197 PDVCY-SWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLGE 263
Cdd:COG5029   92 AGSTYhTYLATLLAELLGR-PPPDPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGALRALGA 157
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
26-69 1.52e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 49.82  E-value: 1.52e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 254553295   26 MNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYD 69
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 180-269 8.70e-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: 49.12  E-value: 8.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 180 CERQLPSGGLNGRPEKLpdvCYSWWVLASLKIIGR-LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGL 258
Cdd:cd02890   11 CLKLLPSSYTSLDASRL---WLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSL 87

                         90
                 ....*....|.
gi 254553295 259 SLLGEEQIKPV 269
Cdd:cd02890   88 AILGDDALSRI 98
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 110-263 2.63e-06

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 48.24  E-value: 2.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 110 VATLALLGKLDAINVEK-AIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFL-AITSQ--LHQVNSDLLGWWLCERQLP 185
Cdd:PLN02710  79 LHSIALLGESLDDELENdTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLvTIGGEraLSSINREKLYTFLLRMKDP 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 186 SGGLNGRPEKLPDV--CYSWWVLASLkiigrLHWIDRE---KLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSL 260
Cdd:PLN02710 159 SGGFRMHDGGEMDVraCYTAISVASL-----LNILDDElvkGVGDYILSCQTYE-GGIGGEPGAEAHGGYTFCGLAAMIL 232


                 ...
gi 254553295 261 LGE 263
Cdd:PLN02710 233 INE 235
PLN03012 PLN03012
Camelliol C synthase
 58-142 6.30e-06

Camelliol C synthase


Pssm-ID: 166653 [Multi-domain]  Cd Length: 759  Bit Score: 47.32  E-value: 6.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  58 TLSAVQILTLYDSVH--------VINVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKA 127
Cdd:PLN03012 566 TSSAIQALILFKQLYpdhrteeiNAFIKKAAEYIENIQMLDGSWYGN-WGICFTYGTWFALAGLAAAGKTfnDCEAIRKG 644

                         90
                 ....*....|....*
gi 254553295 128 IEFVLSCMNFDGGFG 142
Cdd:PLN03012 645 VHFLLAAQKDNGGWG 659
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 11-120 2.49e-05

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 44.70  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  11 YWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISA--SIGhDPHLLYTLSAvqILTLYD-SVHVINVDKVVAYVQSLQ 87
Cdd:COG5029  146 AAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYntRIG-EADLLSTFTA--ILTLYDlGAAPKLVDDLQAYILSLQ 222

                         90       100       110
                 ....*....|....*....|....*....|....
gi 254553295  88 KEDGSFAGDIWGEI-DTRFSFCAVATLALLGKLD 120
Cdd:COG5029  223 LPDGGFEGAPWDGVeDVEYTFYGVGALALLGALA 256
PLN02993 PLN02993
lupeol synthase
 58-150 1.31e-04

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 43.36  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  58 TLSAVQILTLYDSVH--------VINVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKA 127
Cdd:PLN02993 566 TSAVIQALVLFKQLYpdhrtkeiIKSIEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAGKTynDCLAMRKG 644

                         90       100
                 ....*....|....*....|...
gi 254553295 128 IEFVLSCMNFDGGFGcrpgsESH 150
Cdd:PLN02993 645 VHFLLTIQRDDGGWG-----ESY 662
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 75-142 2.31e-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: 42.43  E-value: 2.31e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   75 NVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKAIEFVLSCMNFDGGFG 142
Cdd:TIGR01787 461 VLERALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWLLSRQMPDGGWG 529
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 58-187 8.35e-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: 40.28  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295  58 TLSAVQILTL---YDSVHVINVDKVVA----YVQSLQKEDGSFAGDiWGeID----TRFSFCAvatLALLGKLDAIN-VE 125
Cdd:cd02889  168 TGSVLEALGLfgkLYPEHRREIDPAIRravkYLEREQEPDGSWYGR-WG-VCfiygTWFALEA---LAAAGEDENSPyVR 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295 126 KAIEFVLSCMNFDGGFG--CrpgsESHAGQIYCCTGflaiTSQLHQVnsdllGW---------------------WLCER 182
Cdd:cd02889  243 KACDWLLSKQNPDGGWGesY----ESYEDPSYAGGG----RSTVVQT-----AWallalmaagepdseavkrgvkYLLNT 309


                 ....*
gi 254553295 183 QLPSG 187
Cdd:cd02889  310 QQEDG 314
osq_cycl TIGR03463
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ...
 76-188 2.34e-03

2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella aurantiaca which produces cycloartenol, and Gemmata obscuriglobus and Methylococcus capsulatus, which each produce the closely related sterol, lanosterol.


Pssm-ID: 274591 [Multi-domain]  Cd Length: 634  Bit Score: 39.21  E-value: 2.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553295   76 VDKVVAYVQSLQKEDGSFAGdIWGEIDTRFSFCAVATLALLG-KLDAINVEKAIEFVLSCMNFDGGFG-----CRPGS-- 147
Cdd:TIGR03463 479 IRKAEEFIRRRQLDDGSFMG-FWGICFTYATFFGAKGLIAAGaEPADMALQAAAAFLLEKQRADGAWGehvesCLEARwv 557

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 254553295  148 ESHAGQIYCCTGFLAITSQLHQVNSDLLG---WWLCERQLPSGG 188
Cdd:TIGR03463 558 EGKHGHAVMTAWALLALAAAGEAAHDAAErgiAWLCEQQGEDGG 601
hopene_cyclase TIGR01507
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ...
 76-142 4.32e-03

squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) biosynthesis. Squalene hopene cyclase, an integral membrane protein, directly cyclizes squalene into hopanoid products. [Fatty acid and phospholipid metabolism, Other]


Pssm-ID: 273661 [Multi-domain]  Cd Length: 635  Bit Score: 38.33  E-value: 4.32e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254553295   76 VDKVVAYVQSLQKEDGSFAGDiWGeidTRFSFCAVATLALLGKLDAIN----VEKAIEFVLSCMNFDGGFG 142
Cdd:TIGR01507 473 IERAVEYLKREQEPDGSWFGR-WG---VNYLYGTGAVLSALKAVGIDTrepyIQKALAWLESHQNPDGGWG 539
 
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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