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Conserved domains on  [gi|78099082|sp|Q8BUY9|]
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RecName: Full=Geranylgeranyl transferase type-1 subunit beta; AltName: Full=Geranylgeranyl transferase type I subunit beta; Short=GGTase-I-beta; AltName: Full=Type I protein geranyl-geranyltransferase subunit beta

Protein Classification

geranylgeranyl transferase type-1 subunit beta( domain architecture ID 10121027)

geranylgeranyl transferase type-1 subunit beta catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to a cysteine at the fourth position from the C-terminus of proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X

CATH:  1.25.40.120
EC:  2.5.1.59
Gene Ontology:  GO:0005953|GO:0004661|GO:0004662|GO:0018344|GO:0008270
PubMed:  8621375
SCOP:  4001193

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 22-332 4.21e-172

Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I ). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity.


:

Pssm-ID: 239225 [Multi-domain]  Cd Length: 307  Bit Score: 481.78  E-value: 4.21e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLD---VVNKDDIIEWIYSLQVLptedrSNLSRCGFRGS 98
Cdd:cd02895   1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDsilVEEKDDIIEWIYSLQVL-----SNLPRGGFRGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  99 SYLGIPfnpsknpGAAHPYDSGHIAMTYTGLSCLIILGDDLGRVDKEACLAGLRALQLEDGSFCAV--PEGSENDMRFVY 176
Cdd:cd02895  76 STLGLP-------GTASKYDTGNLAMTYFALLSLLILGDDLSRVDRKAILNFLSKLQLPDGSFGSVldSEGGENDMRFCY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 177 CASCICYMLNNWS--GMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEvFSEKELNRIKRWCIM 254
Cdd:cd02895 149 CAVAICYMLDDWSeeDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE-LSEKFLERLKRWLVH 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 255 RQQN--GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02895 228 RQVSgtGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
 
Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 22-332 4.21e-172

Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I ). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity.


Pssm-ID: 239225 [Multi-domain]  Cd Length: 307  Bit Score: 481.78  E-value: 4.21e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLD---VVNKDDIIEWIYSLQVLptedrSNLSRCGFRGS 98
Cdd:cd02895   1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDsilVEEKDDIIEWIYSLQVL-----SNLPRGGFRGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  99 SYLGIPfnpsknpGAAHPYDSGHIAMTYTGLSCLIILGDDLGRVDKEACLAGLRALQLEDGSFCAV--PEGSENDMRFVY 176
Cdd:cd02895  76 STLGLP-------GTASKYDTGNLAMTYFALLSLLILGDDLSRVDRKAILNFLSKLQLPDGSFGSVldSEGGENDMRFCY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 177 CASCICYMLNNWS--GMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEvFSEKELNRIKRWCIM 254
Cdd:cd02895 149 CAVAICYMLDDWSeeDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE-LSEKFLERLKRWLVH 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 255 RQQN--GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02895 228 RQVSgtGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-354 9.53e-49

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 167.18  E-value: 9.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082   14 EGERLDFLRDRHVRFFQRcLQVLPERYSSLETS--RLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQvlpteDRSnls 91
Cdd:PLN03201   2 SGPMGELVVDKHVRYIKS-LEKKKDSFESVVMEhlRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQ-----HES--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082   92 rCGFRGssylgipfNPSKNPgaahpydsgHIAMTytgLSCLIILG--DDLGRVDKEACLAGLRALQLEDGSFcAVPEGSE 169
Cdd:PLN03201  73 -GGFGG--------NTGHDP---------HILYT---LSAVQILAlfDRLDLLDADKVASYVAGLQNEDGSF-SGDEWGE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  170 NDMRFVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsEKELnrIK 249
Cdd:PLN03201 131 IDTRFSYCALCCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHV--DKDL--LG 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  250 RWCIMRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGIC 327
Cdd:PLN03201 207 WWLCERQvkSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVA 286

                        330       340
                 ....*....|....*....|....*..
gi 78099082  328 GLSLMEESGICKVHPALNVSTRTSERL 354
Cdd:PLN03201 287 GLSLLGYPGLKPIDPAYALPVDVVNRI 313
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 112-333 1.48e-12

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 67.04  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 112 GAAHPYDSGHIAMTYTGLSCLIILGDDlgRVDKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCAScICYMLNNWSGM 191
Cdd:COG5029  37 GFAGRSGPSDLYSTYYAVRTLALLGES--PKWRDRVADLLSSLRVEDGGFAKAPEGGAGSTYHTYLAT-LLAELLGRPPP 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 192 DMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEevfsEKELNRIKRWCIMRQQN--GYHGRPNKPV- 268
Cdd:COG5029 114 DPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD----DPIETKVIRFLRDVQSPegGFAYNTRIGEa 189

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78099082 269 DTCYSFWVGATLKLLKIfQYTNFEKNRNYILSTQdRLVGGFAKWP-DSHPDALHAYFGICGLSLME 333
Cdd:COG5029 190 DLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQ-LPDGGFEGAPwDGVEDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
191-234 9.15e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 47.89  E-value: 9.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 78099082   191 MDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMG 234
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
 
Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 22-332 4.21e-172

Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-I s are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-I ). GGTase-I prenylates the cysteine in the terminal sequence, "CAAX" when X is Leu or Phe. Substrates for GTTase-I include the gamma subunit of neural G-proteins and several Ras-related G-proteins. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity.


Pssm-ID: 239225 [Multi-domain]  Cd Length: 307  Bit Score: 481.78  E-value: 4.21e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLD---VVNKDDIIEWIYSLQVLptedrSNLSRCGFRGS 98
Cdd:cd02895   1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDsilVEEKDDIIEWIYSLQVL-----SNLPRGGFRGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  99 SYLGIPfnpsknpGAAHPYDSGHIAMTYTGLSCLIILGDDLGRVDKEACLAGLRALQLEDGSFCAV--PEGSENDMRFVY 176
Cdd:cd02895  76 STLGLP-------GTASKYDTGNLAMTYFALLSLLILGDDLSRVDRKAILNFLSKLQLPDGSFGSVldSEGGENDMRFCY 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 177 CASCICYMLNNWS--GMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEvFSEKELNRIKRWCIM 254
Cdd:cd02895 149 CAVAICYMLDDWSeeDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE-LSEKFLERLKRWLVH 227

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 255 RQQN--GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02895 228 RQVSgtGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 22-332 2.44e-133

Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The protein prenyltransferase family of lipid-modifying enzymes includes protein farnesyltransferase (FTase) and geranylgeranyltransferase types I and II (GGTase-I and GGTase-II). They catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between the C1 atom of farnesyl (15-carbon by FTase) or geranylgeranyl (20-carbon by GGTase-I, II) isoprenoid lipids and cysteine residues at or near the C-terminus of protein acceptors. FTase and GGTase-I prenylate the cysteine in the terminal sequence, "CAAX"; and GGTase-II prenylates both cysteines in the "CC" (or "CXC") terminal sequence. These enzymes are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTase-II does not recognize its protein acceptor directly but requires Rab to complex with REP (Rab escort protein) before prenylation can occur. These enzymes are found exclusively in eukaryotes.


Pssm-ID: 239220 [Multi-domain]  Cd Length: 286  Bit Score: 382.70  E-value: 2.44e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDS-LDVVNKDDIIEWIYSLQVLPTedrsnlsrCGFRGSsy 100
Cdd:cd02890   1 REKHIKYLQRCLKLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNED--------GGFGGG-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 101 lgipfnpsknpgaahPYDSGHIAMTYTGLSCLIILGDD-LGRVDKEACLAGLRALQLEDGSFCAVPEGsENDMRFVYCAS 179
Cdd:cd02890  71 ---------------PGQDPHLASTYAAVLSLAILGDDaLSRIDREKIYKFLSSLQNPDGSFRGDLGG-EVDTRFVYCAL 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 180 CICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFsekeLNRIKRWCIMRQQN- 258
Cdd:cd02890 135 SILSLLNILTDIDKEKLIDYILSCQNYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLID----KERLLRWLVERQLAs 210

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78099082 259 --GYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSLM 332
Cdd:cd02890 211 ggGFNGRPNKLVDTCYSFWVGASLKILGRLHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 22-332 5.31e-61

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: 198.54  E-value: 5.31e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDML------DSLDVVNKDDIIEWIYSLQvlptedrsnLSRCGF 95
Cdd:cd00688   1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLlaatgiRDKADENIEKGIQRLLSYQ---------LSDGGF 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  96 RGSSYlgipfnpsknpgaahpYDSGHIAMTYTGLSCLIILGDD--LGRVDKEACLAGLRALQLEDGSFCAV------PEG 167
Cdd:cd00688  72 SGWGG----------------NDYPSLWLTAYALKALLLAGDYiaVDRIDLARALNWLLSLQNEDGGFREDgpgnhrIGG 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 168 SENDMRFVYCASCICYMLNNWS-GMDMKKAISYIRRSMSYDNGLaqGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELn 246
Cdd:cd00688 136 DESDVRLTAYALIALALLGKLDpDPLIEKALDYLLSCQNYDGGF--GPGGESHGYGTACAAAALALLGDLDSPDAKKAL- 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 247 rikRWCIMRQQNGYHG-----RPNKPVDTCYSFWVGATLK-LLKIFQYTNFEKNRNYILStQDRLVGGFAKWPDSHPDAL 320
Cdd:cd00688 213 ---RWLLSRQRPDGGWgegrdRTNKLSDSCYTEWAAYALLaLGKLGDLEDAEKLVKWLLS-QQNEDGGFSSKPGKSYDTQ 288

                       330
                ....*....|..
gi 78099082 321 HAYFGICGLSLM 332
Cdd:cd00688 289 HTVFALLALSLY 300
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 20-332 2.84e-57

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: 188.25  E-value: 2.84e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  20 FLRDRHVRFFQrclQVLPERYSS----LETSRLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQVLPTEdrsnlsrcGF 95
Cdd:cd02894   1 LLLEKHIEYIL---SLTKKKDDYeyilTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQDNEDG--------GF 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  96 rgssylgipfnpSKNPGaahpYDSgHIAMTYTGLSCLIILgDDLGRVD--KEACLAGLRALQLEDGSFCAVPEGsENDMR 173
Cdd:cd02894  70 ------------GGSPG----HDP-HILSTLSAIQILALY-DLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWG-EVDTR 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 174 FVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEkelnRIKRWCI 253
Cdd:cd02894 131 FSYCAVLCLTLLGKLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRD----RLGWWLC 206

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 254 MRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGICGLSL 331
Cdd:cd02894 207 ERQlpSGGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSL 286


                .
gi 78099082 332 M 332
Cdd:cd02894 287 L 287
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 22-331 1.30e-55

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


Pssm-ID: 239223 [Multi-domain]  Cd Length: 299  Bit Score: 184.36  E-value: 1.30e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  22 RDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLDSLDVVN-KDDIIEWIYSLQvlPTEDrsnlsrcGFRGSsy 100
Cdd:cd02893   1 REKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSyADDVISFLRRCQ--NPSG-------GFGGG-- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 101 lgipfnpsknpgaahPYDSGHIAMTYTGLSCLIILGDD--LGRVDKEACLAGLRALQLEDGSFcAVPEGSENDMRFVYCA 178
Cdd:cd02893  70 ---------------PGQLPHLATTYAAVNALAIIGTEeaYDVIDREALYKFLLSLKQPDGSF-RMHVGGEVDVRGTYCA 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 179 SCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsekELNRIKRWCIMRQQN 258
Cdd:cd02893 134 ISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKL----DLESLLRWLVARQMR 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 259 ---GYHGRPNKPVDTCYSFWVGATLKLLK-------------IFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHA 322
Cdd:cd02893 210 fegGFQGRTNKLVDGCYSFWVGGSLPILEailnaekkfddsaEGTLFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHT 289


                ....*....
gi 78099082 323 YFGICGLSL 331
Cdd:cd02893 290 CYALSGLSI 298
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-354 9.53e-49

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 167.18  E-value: 9.53e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082   14 EGERLDFLRDRHVRFFQRcLQVLPERYSSLETS--RLTIAFFALSGLDMLDSLDVVNKDDIIEWIYSLQvlpteDRSnls 91
Cdd:PLN03201   2 SGPMGELVVDKHVRYIKS-LEKKKDSFESVVMEhlRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQ-----HES--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082   92 rCGFRGssylgipfNPSKNPgaahpydsgHIAMTytgLSCLIILG--DDLGRVDKEACLAGLRALQLEDGSFcAVPEGSE 169
Cdd:PLN03201  73 -GGFGG--------NTGHDP---------HILYT---LSAVQILAlfDRLDLLDADKVASYVAGLQNEDGSF-SGDEWGE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  170 NDMRFVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsEKELnrIK 249
Cdd:PLN03201 131 IDTRFSYCALCCLSLLKRLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHV--DKDL--LG 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  250 RWCIMRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLKIFQYTNFEKNRNYILSTQDRLVGGFAKWPDSHPDALHAYFGIC 327
Cdd:PLN03201 207 WWLCERQvkSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVA 286

                        330       340
                 ....*....|....*....|....*..
gi 78099082  328 GLSLMEESGICKVHPALNVSTRTSERL 354
Cdd:PLN03201 287 GLSLLGYPGLKPIDPAYALPVDVVNRI 313
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 17-284 3.82e-31

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 122.59  E-value: 3.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082   17 RLDFLRDRHVRFFQRCLQVLPERYSSLETSRLTIAFFALSGLDMLD-SLDVVNKDDIIEWiyslqvlptedrsnLSRCGF 95
Cdd:PLN02710  41 MLELWREKHLEYLTRGLRQLGPSFSVLDANRPWLCYWILHSIALLGeSLDDELENDTIDF--------------LSRCQD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082   96 RGSSYLGipfNPSKNPgaahpydsgHIAMTYTGLSCLIILGDD--LGRVDKEACLAGLRALQLEDGSFcAVPEGSENDMR 173
Cdd:PLN02710 107 PNGGYGG---GPGQLP---------HLATTYAAVNTLVTIGGEraLSSINREKLYTFLLRMKDPSGGF-RMHDGGEMDVR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  174 FVYCASCICYMLNNWSGMDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVfsekELNRIKRWCI 253
Cdd:PLN02710 174 ACYTAISVASLLNILDDELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRL----DLPSLINWVV 249

                        250       260       270
                 ....*....|....*....|....*....|...
gi 78099082  254 MRQ--QNGYHGRPNKPVDTCYSFWVGATLKLLK 284
Cdd:PLN02710 250 FRQgvEGGFQGRTNKLVDGCYSFWQGGVFALLQ 282
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 112-333 1.48e-12

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 67.04  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 112 GAAHPYDSGHIAMTYTGLSCLIILGDDlgRVDKEACLAGLRALQLEDGSFCAVPEGSENDMRFVYCAScICYMLNNWSGM 191
Cdd:COG5029  37 GFAGRSGPSDLYSTYYAVRTLALLGES--PKWRDRVADLLSSLRVEDGGFAKAPEGGAGSTYHTYLAT-LLAELLGRPPP 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 192 DMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMGKLEevfsEKELNRIKRWCIMRQQN--GYHGRPNKPV- 268
Cdd:COG5029 114 DPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD----DPIETKVIRFLRDVQSPegGFAYNTRIGEa 189

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78099082 269 DTCYSFWVGATLKLLKIfQYTNFEKNRNYILSTQdRLVGGFAKWP-DSHPDALHAYFGICGLSLME 333
Cdd:COG5029 190 DLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQ-LPDGGFEGAPwDGVEDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
191-234 9.15e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 47.89  E-value: 9.15e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 78099082   191 MDMKKAISYIRRSMSYDNGLAQGAGLESHGGSTFCGIASLCLMG 234
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
290-333 5.67e-07

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 45.58  E-value: 5.67e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 78099082   290 NFEKNRNYILSTQdRLVGGFAKWPDSHPDALHAYFGICGLSLME 333
Cdd:pfam00432   2 DKEKLVDYLLSCQ-NEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
240-283 5.11e-06

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 42.88  E-value: 5.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 78099082   240 FSEKELNRIKRWCiMRQQNGYHGRPNKPVDTCYSFWVGATLKLL 283
Cdd:pfam00432   1 IDKEKLVDYLLSC-QNEDGGFGGRPGGESDTYYTYCALAALALL 43
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 21-238 6.77e-06

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 47.01  E-value: 6.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  21 LRDRHVRFFQRCLQV---LPER--YSSLETSrltiaFFALSGLDMLdSLDVVNKDDIIEWIYSLQV-------LPTEDRS 88
Cdd:COG5029  20 FTDSHLDYLRASQNPdggFAGRsgPSDLYST-----YYAVRTLALL-GESPKWRDRVADLLSSLRVedggfakAPEGGAG 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  89 NLSRCGF--RGSSYLGIPFN-PSK---------NPGAAHPYDSGHIA---MTYTGLSCLIILGDdLGRVDKEACLAGLRA 153
Cdd:COG5029  94 STYHTYLatLLAELLGRPPPdPDRlvrflisqqNDDGGFEISPGRRSdtnPTAAAIGALRALGA-LDDPIETKVIRFLRD 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 154 LQLEDGSFCAVPEGSENDMRFVYCASCICYMLNNWSGMDmKKAISYIRrSMSYDNGLAQGAGLESHG--GSTFCGIASLC 231
Cdd:COG5029 173 VQSPEGGFAYNTRIGEADLLSTFTAILTLYDLGAAPKLV-DDLQAYIL-SLQLPDGGFEGAPWDGVEdvEYTFYGVGALA 250


                ....*..
gi 78099082 232 LMGKLEE 238
Cdd:COG5029 251 LLGALAE 257
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
142-186 8.02e-06

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 42.50  E-value: 8.02e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 78099082   142 VDKEACLAGLRALQLEDGSFCAVPEGsENDMRFVYCASCICYMLN 186
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGG-ESDTYYTYCALAALALLG 44
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
113-334 1.04e-04

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 43.56  E-value: 1.04e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 113 AAHPYDSGHIAMTYTGLSCLIILGDDLGRVDKeaCLAGLRALQLEDGSFCAVpegsendmrfvYCASCICYMLNnwsgmD 192
Cdd:COG1689  26 CAYPGLPSTLADTYYAVRILKLLGEEVPNRDK--TIEFLESCQDEEGGGFAL-----------YTTSYGLMALA-----L 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082 193 MKKAISYIRRSMSY--DNGLAQGAGLESHGGSTFCGIASLCLMGKLEEVFSEKELNRIKrwciMRQQNGYHGRpnKPVDT 270
Cdd:COG1689  88 LGIDPPDEQEALEYlsDALPTKFAGGASDLEETYLAVALLEALGASEPEREKIREFLLS----LRRPDGGFGG--KKPNL 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78099082 271 CYSFWVGATLKLLKIfQYTNFEKNRNYILSTQDRlVGGFAKWPDSHPDALHAYFGICGLSLMEE 334
Cdd:COG1689 162 EDTYWALAALRRLGR-DLPPADRVIAFILACQNE-DGGFSKTPGSYSDLEATYYALRALKLLGE 223
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
48-167 3.71e-03

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 38.55  E-value: 3.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78099082  48 LTIAFFALSGLDMLDSlDVVNKDDIIEWIYSLQvlpTEDRsnlsrcGFrgssylgipfnpSKNPGAaHPYdsghIAMTYT 127
Cdd:COG1689 161 LEDTYWALAALRRLGR-DLPPADRVIAFILACQ---NEDG------GF------------SKTPGS-YSD----LEATYY 213

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 78099082 128 GLSCLIILGDDLGRVDKeaCLAGLRALQLEDGSFCAVPEG 167
Cdd:COG1689 214 ALRALKLLGEPPKNVDK--LLEFIASCQNSDGGFRRSPEG 251
 
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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