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Conserved domains on  [gi|254553291|ref|NP_035361|]
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geranylgeranyl transferase type-2 subunit beta isoform 1 [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 ...
 26-309 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: 544.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  26 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQ-HECGGISASIGHDPHLL 104
Cdd:cd02894    1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 105 YTLSAVQILTLYDSVHVI--NVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSC 182
Cdd:cd02894   81 STLSAIQILALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 183 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 262
Cdd:cd02894  161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 254553291 263 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:cd02894  241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 26-309 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: 544.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  26 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQ-HECGGISASIGHDPHLL 104
Cdd:cd02894    1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 105 YTLSAVQILTLYDSVHVI--NVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSC 182
Cdd:cd02894   81 STLSAIQILALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 183 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 262
Cdd:cd02894  161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 254553291 263 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:cd02894  241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 22-331 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 513.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  22 APDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDP 101
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 102 HLLYTLSAVQILTLYDSVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLS 181
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 182 CMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 261
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 262 RLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRV 331
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 76-310 2.00e-28

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: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  76 REEILVFIKSCQHECGGISASIGhDPHLLYTLSAVQILTLYDSVHVINvDKVVAYVQSLQKEDGSFA-------GDIWGe 148
Cdd:COG5029   21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 149 idtrfSFCAVATLALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLC 228
Cdd:COG5029   98 -----TYLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 229 ERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGL 306
Cdd:COG5029  172 DVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGAL 249


                 ....
gi 254553291 307 SLLG 310
Cdd:COG5029  250 ALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
170-211 2.57e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.60  E-value: 2.57e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 254553291  170 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 211
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 123-190 3.16e-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: 3.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  123 NVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKAIEFVLSCMNFDGGFG 190
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 ...
 26-309 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: 544.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  26 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQ-HECGGISASIGHDPHLL 104
Cdd:cd02894    1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 105 YTLSAVQILTLYDSVHVI--NVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSC 182
Cdd:cd02894   81 STLSAIQILALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 183 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 262
Cdd:cd02894  161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 254553291 263 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:cd02894  241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 22-331 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 513.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  22 APDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISASIGHDP 101
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 102 HLLYTLSAVQILTLYDSVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLS 181
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 182 CMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 261
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 262 RLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRV 331
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 28-309 3.09e-148

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: 418.91  E-value: 3.09e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  28 LEKHADYIASYGsKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQ-LHRMNREEILVFIKSCQ-HECGGISASIGHDPHLLY 105
Cdd:cd02890    1 REKHIKYLQRCL-KLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHLAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 106 TLSAVQILTLYDS--VHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCM 183
Cdd:cd02890   80 TYAAVLSLAILGDdaLSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 184 NFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSG-GLNGRPEKLPDVCYSWWVLASLKIIGR 262
Cdd:cd02890  160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKILGR 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 254553291 263 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:cd02890  240 LHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 28-309 7.34e-77

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: 237.83  E-value: 7.34e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  28 LEKHADYIASYGsKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLH------RMNREEILVFIKSCQHECGGISASIGHD- 100
Cdd:cd00688    1 IEKHLKYLLRYP-YGDGHWYQSLCGEQTWSTAWPLLALLLLLAATgirdkaDENIEKGIQRLLSYQLSDGGFSGWGGNDy 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 101 PHLLYTLSAVQILTL---YDSVHVINVDKVVAYVQSLQKEDGSFAGDIWG-------EIDTRFSFCAVATLALLGKLDA- 169
Cdd:cd00688   80 PSLWLTAYALKALLLagdYIAVDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDPd 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 170 INVEKAIEFVLSCMNFDGGFGcrPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPE---KLPD 246
Cdd:cd00688  160 PLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnKLSD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254553291 247 VCYSWWVLASLKIIGRL-HWIDREKLRSFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:cd00688  238 SCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 54-309 1.23e-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: 217.15  E-value: 1.23e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  54 RMSGVYWGLTVMDLMGQLHRM---NREEILVFIKSCQ----HECGGISASIGHD----------PHLLYTLSAVQIL-TL 115
Cdd:cd02895   26 RLTIAFFALSGLDLLGALDSIlveEKDDIIEWIYSLQvlsnLPRGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLlIL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 116 YDSVHVINVDKVVAYVQSLQKEDGSFAGDIW---GEIDTRFSFCAVATLALLG--KLDAINVEKAIEFVLSCMNFDGGFG 190
Cdd:cd02895  106 GDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYMLDdwSEEDIDKEKLIDYIKSSQSYDGGFG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 191 CRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGW---WLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWID 267
Cdd:cd02895  186 QGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERlkrWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLID 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 254553291 268 REKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:cd02895  266 FEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 58-308 3.35e-64

Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). FTases are a subgroup of PTase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. These proteins are heterodimers of alpha and beta subunits. Both subunits are required for catalytic activity. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids. Ftase attaches a 15-carbon farnesyl group to the cysteine within the C-terminal CaaX motif of substrate proteins when X is Ala, Met, Ser, Cys or Gln. Protein farnesylation has been shown to play critical roles in a variety of cellular processes including Ras/mitogen activated protein kinase signaling pathways in mammals and, abscisic acid signal transduction in Arabidopsis.


Pssm-ID: 239223 [Multi-domain]  Cd Length: 299  Bit Score: 205.55  E-value: 3.35e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  58 VYWGLTVMDLMG-QLHRMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTL---YDSVHVINVDKVVAYVQS 133
Cdd:cd02893   30 LYWILHSLELLGeELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTYAAVNALAIigtEEAYDVIDREALYKFLLS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 134 LQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITS 213
Cdd:cd02893  110 LKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 214 QLHQVNSDLLGWWLCERQLPS-GGLNGRPEKLPDVCYSWWVLASLKIIGRL------------HW-IDREKLRSFILACQ 279
Cdd:cd02893  190 KPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPILEAIlnaekkfddsaeGTlFDQEALQEYILLCC 269

                        250       260
                 ....*....|....*....|....*....
gi 254553291 280 DEETGGFADRPGDMVDPFHTLFGIAGLSL 308
Cdd:cd02893  270 QSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 29-307 2.09e-30

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 119.89  E-value: 2.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  29 EKHADYIASyGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNRE-EILVFIKSCQHECGGISASIGHDPHLLYTL 107
Cdd:PLN02710  47 EKHLEYLTR-GLRQLGPSFSVLDANRPWLCYWILHSIALLGESLDDELEnDTIDFLSRCQDPNGGYGGGPGQLPHLATTY 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 108 SAVQIL-TL--YDSVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMN 184
Cdd:PLN02710 126 AAVNTLvTIggERALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 185 FDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLH 264
Cdd:PLN02710 206 YEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFALLQQLV 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 265 WIDREK-----------------------------------------------------------LRSFILACQDEETGG 285
Cdd:PLN02710 286 TIVDEQlqtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnqqmgplfhsiaLQQYILLCSQVLDGG 365

                        330       340
                 ....*....|....*....|..
gi 254553291 286 FADRPGDMVDPFHTLFGIAGLS 307
Cdd:PLN02710 366 LRDKPGKSRDYYHTCYCLSGLS 387
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 76-310 2.00e-28

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: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  76 REEILVFIKSCQHECGGISASIGhDPHLLYTLSAVQILTLYDSVHVINvDKVVAYVQSLQKEDGSFA-------GDIWGe 148
Cdd:COG5029   21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 149 idtrfSFCAVATLALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLC 228
Cdd:COG5029   98 -----TYLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLR 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 229 ERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGL 306
Cdd:COG5029  172 DVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGAL 249


                 ....
gi 254553291 307 SLLG 310
Cdd:COG5029  250 ALLG 253
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 20-263 1.14e-20

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 89.77  E-value: 1.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  20 SDAPDTLLLEKHADYIASygSKKDDyeycmSEYLRMSG------VYWGLTVMDLMGQLHRmNREEILVFIKSCQHECGG- 92
Cdd:COG5029   13 SSKSTADFTDSHLDYLRA--SQNPD-----GGFAGRSGpsdlysTYYAVRTLALLGESPK-WRDRVADLLSSLRVEDGGf 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  93 ------ISASIGHdpHLLYTLSAVqiltLYDsVHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGK 166
Cdd:COG5029   85 akapegGAGSTYH--TYLATLLAE----LLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 167 LDAINVEKAIEFVLSCMNFDGGFGCRPgSESHAGQIYCCTGfLAITSQLHQVNSDL--LGWWLCERQLPSGGLNGRP-EK 243
Cdd:COG5029  158 LDDPIETKVIRFLRDVQSPEGGFAYNT-RIGEADLLSTFTA-ILTLYDLGAAPKLVddLQAYILSLQLPDGGFEGAPwDG 235

                        250       260
                 ....*....|....*....|
gi 254553291 244 LPDVCYSWWVLASLKIIGRL 263
Cdd:COG5029  236 VEDVEYTFYGVGALALLGAL 255
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
73-312 1.68e-20

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: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  73 RMNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDsVHVINVDKVVAYVQSLQKEDGSFAGdiwgeidTR 152
Cdd:COG1689    5 RFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLG-EEVPNRDKTIEFLESCQDEEGGGFA-------LY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 153 FSFCAVATLALLGKLDAINVEkAIEFvLSCMNFDGgfgcRPGSESHAGQIYCCT-GFLAitsqLHQVNSDLLGW--WLCE 229
Cdd:COG1689   77 TTSYGLMALALLGIDPPDEQE-ALEY-LSDALPTK----FAGGASDLEETYLAVaLLEA----LGASEPEREKIreFLLS 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 230 RQLPSGGLNGrpeKLPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 309
Cdd:COG1689  147 LRRPDGGFGG---KKPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQN-EDGGFSKTPGSYSDLEATYYALRALKLL 221


                 ...
gi 254553291 310 GEE 312
Cdd:COG1689  222 GEP 224
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
58-193 2.02e-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: 2.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  58 VYWGLTVMDLMGQLHRMnREEILVFIKSCQHECGGISASighDPHLLYTLSAVQILTLYDsVHVINVDKVVAYVQSLQKE 137
Cdd:COG1689  120 TYLAVALLEALGASEPE-REKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRLG-RDLPPADRVIAFILACQNE 194

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 254553291 138 DGSFA---GDIWgeiDTRFSFCAVATLALLGKlDAINVEKAIEFVLSCMNFDGGFGCRP 193
Cdd:COG1689  195 DGGFSktpGSYS---DLEATYYALRALKLLGE-PPKNVDKLLEFIASCQNSDGGFRRSP 249
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
170-211 2.57e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.60  E-value: 2.57e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 254553291  170 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 211
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
26-263 4.80e-12

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 65.52  E-value: 4.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  26 LLLEKHADYIASygSKKDDYEYCMSEYLRMS--GVYWGLTVMDLMGqlHRM-NREEILVFIKSCQHECGGISASIGhdph 102
Cdd:COG1689    6 FDLARTIEYVLK--RQNEDGGFCAYPGLPSTlaDTYYAVRILKLLG--EEVpNRDKTIEFLESCQDEEGGGFALYT---- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 103 LLYTLSAVQIL--TLYDSVHVIN------------------------------------VDKVVAYVQSLQKEDGSFAGD 144
Cdd:COG1689   78 TSYGLMALALLgiDPPDEQEALEylsdalptkfaggasdleetylavallealgasepeREKIREFLLSLRRPDGGFGGK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 145 IWGEIDTRFsfcAVATLALLGKlDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLg 224
Cdd:COG1689  158 KPNLEDTYW---ALAALRRLGR-DLPPADRVIAFILACQNEDGGFSKTPGSYSDLEATYYALRALKLLGEPPKNVDKLL- 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 254553291 225 WWLCERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRL 263
Cdd:COG1689  233 EFIASCQNSDGGFRRSPEGgISTLEYTYYALAVLKWLKRL 272
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
122-165 4.73e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.14  E-value: 4.73e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 254553291  122 INVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLG 165
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
218-261 5.64e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 56.75  E-value: 5.64e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 254553291  218 VNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 261
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
266-310 9.71e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 56.37  E-value: 9.71e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 254553291  266 IDREKLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLG 310
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 166-311 1.53e-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: 1.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 166 KLDAINVEKAIEFVLSCMNFDGGFGCRPGsESHAGQIYCCTGFLAITSQLHQVNSDLLGWWL-CERqlPSGGLNGRPEKL 244
Cdd:COG5029   15 KSTADFTDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRV--EDGGFAKAPEGG 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254553291 245 PDVCY-SWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLGE 311
Cdd:COG5029   92 AGSTYhTYLATLLAELLGR-PPPDPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGALRALGA 157
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
74-117 1.81e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 49.82  E-value: 1.81e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 254553291   74 MNREEILVFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYD 117
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 228-317 1.32e-06

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: 1.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 228 CERQLPSGGLNGRPEKLpdvCYSWWVLASLKIIGR-LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGL 306
Cdd:cd02890   11 CLKLLPSSYTSLDASRL---WLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSL 87

                         90
                 ....*....|.
gi 254553291 307 SLLGEEQIKPV 317
Cdd:cd02890   88 AILGDDALSRI 98
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 158-311 3.80e-06

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 48.24  E-value: 3.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 158 VATLALLGKLDAINVEK-AIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFL-AITSQ--LHQVNSDLLGWWLCERQLP 233
Cdd:PLN02710  79 LHSIALLGESLDDELENdTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLvTIGGEraLSSINREKLYTFLLRMKDP 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 234 SGGLNGRPEKLPDV--CYSWWVLASLkiigrLHWIDRE---KLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSL 308
Cdd:PLN02710 159 SGGFRMHDGGEMDVraCYTAISVASL-----LNILDDElvkGVGDYILSCQTYE-GGIGGEPGAEAHGGYTFCGLAAMIL 232


                 ...
gi 254553291 309 LGE 311
Cdd:PLN02710 233 INE 235
PLN03012 PLN03012
Camelliol C synthase
 106-190 8.95e-06

Camelliol C synthase


Pssm-ID: 166653 [Multi-domain]  Cd Length: 759  Bit Score: 47.32  E-value: 8.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 106 TLSAVQILTLYDSVH--------VINVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKA 175
Cdd:PLN03012 566 TSSAIQALILFKQLYpdhrteeiNAFIKKAAEYIENIQMLDGSWYGN-WGICFTYGTWFALAGLAAAGKTfnDCEAIRKG 644

                         90
                 ....*....|....*
gi 254553291 176 IEFVLSCMNFDGGFG 190
Cdd:PLN03012 645 VHFLLAAQKDNGGWG 659
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 59-168 3.27e-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: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  59 YWGLTVMDLMGQLHRMNREEILVFIKSCQHECGGISA--SIGhDPHLLYTLSAvqILTLYD-SVHVINVDKVVAYVQSLQ 135
Cdd:COG5029  146 AAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYntRIG-EADLLSTFTA--ILTLYDlGAAPKLVDDLQAYILSLQ 222

                         90       100       110
                 ....*....|....*....|....*....|....
gi 254553291 136 KEDGSFAGDIWGEI-DTRFSFCAVATLALLGKLD 168
Cdd:COG5029  223 LPDGGFEGAPWDGVeDVEYTFYGVGALALLGALA 256
PLN02993 PLN02993
lupeol synthase
 106-198 1.82e-04

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 43.36  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 106 TLSAVQILTLYDSVH--------VINVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKA 175
Cdd:PLN02993 566 TSAVIQALVLFKQLYpdhrtkeiIKSIEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAGKTynDCLAMRKG 644

                         90       100
                 ....*....|....*....|...
gi 254553291 176 IEFVLSCMNFDGGFGcrpgsESH 198
Cdd:PLN02993 645 VHFLLTIQRDDGGWG-----ESY 662
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 123-190 3.16e-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: 3.16e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  123 NVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKAIEFVLSCMNFDGGFG 190
Cdd:TIGR01787 461 VLERALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWLLSRQMPDGGWG 529
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 106-235 1.44e-03

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: 39.90  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 106 TLSAVQILTL---YDSVHVINVDKVVA----YVQSLQKEDGSFAGDiWGeID----TRFSFCAvatLALLGKLDAIN-VE 173
Cdd:cd02889  168 TGSVLEALGLfgkLYPEHRREIDPAIRravkYLEREQEPDGSWYGR-WG-VCfiygTWFALEA---LAAAGEDENSPyVR 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291 174 KAIEFVLSCMNFDGGFG--CrpgsESHAGQIYCCTGflaiTSQLHQVnsdllGW---------------------WLCER 230
Cdd:cd02889  243 KACDWLLSKQNPDGGWGesY----ESYEDPSYAGGG----RSTVVQT-----AWallalmaagepdseavkrgvkYLLNT 309


                 ....*
gi 254553291 231 QLPSG 235
Cdd:cd02889  310 QQEDG 314
osq_cycl TIGR03463
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ...
 124-236 2.57e-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: 39.59  E-value: 2.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254553291  124 VDKVVAYVQSLQKEDGSFAGdIWGEIDTRFSFCAVATLALLG-KLDAINVEKAIEFVLSCMNFDGGFG-----CRPGS-- 195
Cdd:TIGR03463 479 IRKAEEFIRRRQLDDGSFMG-FWGICFTYATFFGAKGLIAAGaEPADMALQAAAAFLLEKQRADGAWGehvesCLEARwv 557

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 254553291  196 ESHAGQIYCCTGFLAITSQLHQVNSDLLG---WWLCERQLPSGG 236
Cdd:TIGR03463 558 EGKHGHAVMTAWALLALAAAGEAAHDAAErgiAWLCEQQGEDGG 601
 
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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