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Conserved domains on  [gi|6321283|ref|NP_011360|]
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protein geranylgeranyltransferase type I subunit CDC43 [Saccharomyces cerevisiae S288C]

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 ...
 13-352 4.30e-128

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: 370.07  E-value: 4.30e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   13 TKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSakygdHLGWMRKHYIKTVLDD--TENTVISGFVGS 90
Cdd:cd02895   1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDS-----ILVEEKDDIIEWIYSLqvLSNLPRGGFRGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   91 ----LVMNIPHATTINLPNTLFALLSMIMLRDYEYFetiLDKRSLARFVSKCQRPDrGSFVSCLDyktncgSSVDSDDLR 166
Cdd:cd02895  76 stlgLPGTASKYDTGNLAMTYFALLSLLILGDDLSR---VDRKAILNFLSKLQLPD-GSFGSVLD------SEGGENDMR 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  167 FCYIAVAILYICGCRSKEDfdeyIDTEKLLGYIMSQQCYNGAFGA--HNEPHSGYTSCALSTLALLSSLEKLSDKFKEDT 244
Cdd:cd02895 146 FCYCAVAICYMLDDWSEED----IDKEKLIDYIKSSQSYDGGFGQgpGLESHGGSTFCAIASLSLLGKLEELSEKFLERL 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  245 ITWLLHRQVSSHgcmkfeselnasydqsddgGFQGRENKFADTCYAFWCLNSLHLLTKDwkMLCQTELVTNYLLDrTQKT 324
Cdd:cd02895 222 KRWLVHRQVSGT-------------------GFNGRPNKPADTCYSFWVGASLKLLDAF--QLIDFEKNRNYLLS-TQQS 279

                       330       340
                ....*....|....*....|....*...
gi 6321283  325 LTGGFSKNDEEDADLYHSCLGSAALALI 352
Cdd:cd02895 280 LVGGFAKNPDSHPDPLHSYLGLAALSLI 307
 
Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 13-352 4.30e-128

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: 370.07  E-value: 4.30e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   13 TKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSakygdHLGWMRKHYIKTVLDD--TENTVISGFVGS 90
Cdd:cd02895   1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDS-----ILVEEKDDIIEWIYSLqvLSNLPRGGFRGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   91 ----LVMNIPHATTINLPNTLFALLSMIMLRDYEYFetiLDKRSLARFVSKCQRPDrGSFVSCLDyktncgSSVDSDDLR 166
Cdd:cd02895  76 stlgLPGTASKYDTGNLAMTYFALLSLLILGDDLSR---VDRKAILNFLSKLQLPD-GSFGSVLD------SEGGENDMR 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  167 FCYIAVAILYICGCRSKEDfdeyIDTEKLLGYIMSQQCYNGAFGA--HNEPHSGYTSCALSTLALLSSLEKLSDKFKEDT 244
Cdd:cd02895 146 FCYCAVAICYMLDDWSEED----IDKEKLIDYIKSSQSYDGGFGQgpGLESHGGSTFCAIASLSLLGKLEELSEKFLERL 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  245 ITWLLHRQVSSHgcmkfeselnasydqsddgGFQGRENKFADTCYAFWCLNSLHLLTKDwkMLCQTELVTNYLLDrTQKT 324
Cdd:cd02895 222 KRWLVHRQVSGT-------------------GFNGRPNKPADTCYSFWVGASLKLLDAF--QLIDFEKNRNYLLS-TQQS 279

                       330       340
                ....*....|....*....|....*...
gi 6321283  325 LTGGFSKNDEEDADLYHSCLGSAALALI 352
Cdd:cd02895 280 LVGGFAKNPDSHPDPLHSYLGLAALSLI 307
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 125-353 9.99e-19

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 85.90  E-value: 9.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   125 ILDKRSLARFVSKCQRPDrGSFVscldyktncGSSVDSDDLRFCYIAVAILYICGCRSKedfdeyIDTEKLLGYIMSQQC 204
Cdd:PLN03201 103 LLDADKVASYVAGLQNED-GSFS---------GDEWGEIDTRFSYCALCCLSLLKRLDK------INVEKAVDYIVSCKN 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   205 YNGAFGAH--NEPHSGYTSCALSTLALLSSLEKLsDKfkeDTITW-LLHRQVSShgcmkfeselnasydqsddGGFQGRE 281
Cdd:PLN03201 167 FDGGFGCTpgGESHAGQIFCCVGALAITGSLHHV-DK---DLLGWwLCERQVKS-------------------GGLNGRP 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321283   282 NKFADTCYAFWCLNSLHLLTK-DWkmlCQTELVTNYLLDrTQKTLTGGFSKNDEEDADLYHSCLGSAALALIE 353
Cdd:PLN03201 224 EKLPDVCYSWWVLSSLIIIDRvHW---IDKDKLAKFILD-CQDDENGGISDRPDDAVDVFHTFFGVAGLSLLG 292
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
271-300 5.60e-07

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 45.58  E-value: 5.60e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 6321283    271 QSDDGGFQGRENKFADTCYAFWCLNSLHLL 300
Cdd:pfam00432  14 QNEDGGFGGRPGGESDTYYTYCALAALALL 43
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
124-351 2.61e-03

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 39.32  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  124 TILDKRSLARFVSKCQRPDrGSFvscldyktnCGSSVDSDDLRFCYIAVAILYICGcrskEDFDeyiDTEKLLGYIMSQQ 203
Cdd:COG1689   4 LRFDLARTIEYVLKRQNED-GGF---------CAYPGLPSTLADTYYAVRILKLLG----EEVP---NRDKTIEFLESCQ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  204 CYNGAFGAHNEPHSGYtSCALSTLALLSSLEKLSDKFKEDT------------ITWLLHRQVSSHGCMKFESELNASY-- 269
Cdd:COG1689  67 DEEGGGFALYTTSYGL-MALALLGIDPPDEQEALEYLSDALptkfaggasdleETYLAVALLEALGASEPEREKIREFll 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  270 -DQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDwkmlcQTELVtNYLLDRtQKTlTGGFSKNDEEDADLYHSCLGSAA 348
Cdd:COG1689 146 sLRRPDGGFGGKKPNLEDTYWALAALRRLGRDLPP-----ADRVI-AFILAC-QNE-DGGFSKTPGSYSDLEATYYALRA 217


                ...
gi 6321283  349 LAL 351
Cdd:COG1689 218 LKL 220
 
Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 13-352 4.30e-128

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: 370.07  E-value: 4.30e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   13 TKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSakygdHLGWMRKHYIKTVLDD--TENTVISGFVGS 90
Cdd:cd02895   1 KKKHVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLGALDS-----ILVEEKDDIIEWIYSLqvLSNLPRGGFRGS 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   91 ----LVMNIPHATTINLPNTLFALLSMIMLRDYEYFetiLDKRSLARFVSKCQRPDrGSFVSCLDyktncgSSVDSDDLR 166
Cdd:cd02895  76 stlgLPGTASKYDTGNLAMTYFALLSLLILGDDLSR---VDRKAILNFLSKLQLPD-GSFGSVLD------SEGGENDMR 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  167 FCYIAVAILYICGCRSKEDfdeyIDTEKLLGYIMSQQCYNGAFGA--HNEPHSGYTSCALSTLALLSSLEKLSDKFKEDT 244
Cdd:cd02895 146 FCYCAVAICYMLDDWSEED----IDKEKLIDYIKSSQSYDGGFGQgpGLESHGGSTFCAIASLSLLGKLEELSEKFLERL 221

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  245 ITWLLHRQVSSHgcmkfeselnasydqsddgGFQGRENKFADTCYAFWCLNSLHLLTKDwkMLCQTELVTNYLLDrTQKT 324
Cdd:cd02895 222 KRWLVHRQVSGT-------------------GFNGRPNKPADTCYSFWVGASLKLLDAF--QLIDFEKNRNYLLS-TQQS 279

                       330       340
                ....*....|....*....|....*...
gi 6321283  325 LTGGFSKNDEEDADLYHSCLGSAALALI 352
Cdd:cd02895 280 LVGGFAKNPDSHPDPLHSYLGLAALSLI 307
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 13-352 5.91e-87

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: 264.45  E-value: 5.91e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   13 TKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYgdhlgwmRKHYIKTVLDDTENTvISGFVGSlv 92
Cdd:cd02890   1 REKHIKYLQRCLKLLPSSYTSLDASRLWLLYWILSSLDLLGEDLDDEN-------KDEIIDFIYSCQVNE-DGGFGGG-- 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   93 mnipHATTINLPNTLFALLSMIMLRDYEYfeTILDKRSLARFVSKCQRPDrGSFVSCLdyktncgssVDSDDLRFCYIAV 172
Cdd:cd02890  71 ----PGQDPHLASTYAAVLSLAILGDDAL--SRIDREKIYKFLSSLQNPD-GSFRGDL---------GGEVDTRFVYCAL 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  173 AILYICGCRSkedfdeYIDTEKLLGYIMSQQCYNGAFGA--HNEPHSGYTSCALSTLALLSsleKLSDKFKEDTITWLLH 250
Cdd:cd02890 135 SILSLLNILT------DIDKEKLIDYILSCQNYDGGFGGvpGAESHGGYTFCAVASLALLG---RLDLIDKERLLRWLVE 205

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  251 RQVSSHgcmkfeselnasydqsddGGFQGRENKFADTCYAFWCLNSLHLLTKDWkmLCQTELVTNYLLDrTQKTLTGGFS 330
Cdd:cd02890 206 RQLASG------------------GGFNGRPNKLVDTCYSFWVGASLKILGRLH--LIDQEKLREYILS-CQQSEVGGFS 264

                       330       340
                ....*....|....*....|..
gi 6321283  331 KNDEEDADLYHSCLGSAALALI 352
Cdd:cd02890 265 DKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 13-352 4.81e-43

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: 151.55  E-value: 4.81e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   13 TKKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYGDHLgwMRKHYIKTVLddTENTVISGFVGSLV 92
Cdd:cd00688   1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAATGIRDKADE--NIEKGIQRLL--SYQLSDGGFSGWGG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   93 MNIPHattinLPNTLFALLSMIMLRDYEYFETIlDKRSLARFVSKCQRPDrGSFVSCLDYKTNCGssVDSDDLRFCYIAV 172
Cdd:cd00688  77 NDYPS-----LWLTAYALKALLLAGDYIAVDRI-DLARALNWLLSLQNED-GGFREDGPGNHRIG--GDESDVRLTAYAL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  173 AILYICGCRskedfDEYIDTEKLLGYIMSQQCYNGAFGAHNEPHSGYTSCALstlALLSSLEKLSDKFKEDTITWLLHRQ 252
Cdd:cd00688 148 IALALLGKL-----DPDPLIEKALDYLLSCQNYDGGFGPGGESHGYGTACAA---AALALLGDLDSPDAKKALRWLLSRQ 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  253 VSSHGcmkfeselnasydqsdDGGFQGRENKFADTCYAFWCLNSLhLLTKDWKMLCQTELVTNYLLDrtQKTLTGGFSKN 332
Cdd:cd00688 220 RPDGG----------------WGEGRDRTNKLSDSCYTEWAAYAL-LALGKLGDLEDAEKLVKWLLS--QQNEDGGFSSK 280

                       330       340
                ....*....|....*....|
gi 6321283  333 DEEDADLYHSCLGSAALALI 352
Cdd:cd00688 281 PGKSYDTQHTVFALLALSLY 300
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 14-352 4.00e-32

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: 122.34  E-value: 4.00e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   14 KKHRKFFERHLQLLPSSHQGHDVNRMAIIFYSISGLSIFDVNVSAKYgdhlgwmRKHYIKTVL-DDTENTVISGFVGSlv 92
Cdd:cd02893   2 EKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSY-------ADDVISFLRrCQNPSGGFGGGPGQ-- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   93 mnIPHATTinlpnTLFALLSMIMLRDYEYFETIlDKRSLARFVSKCQRPDrGSFVSCLDYKTncgssvdsdDLRFCYIAV 172
Cdd:cd02893  73 --LPHLAT-----TYAAVNALAIIGTEEAYDVI-DREALYKFLLSLKQPD-GSFRMHVGGEV---------DVRGTYCAI 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  173 AILYICGCRSKEDFDEYIDtekllgYIMSQQCYNGAFGA--HNEPHSGYTSCALSTLALLSSLEKLS-DKFkedtITWLL 249
Cdd:cd02893 135 SVASLLNILTDELFEGVAE------YILSCQTYEGGFGGvpGNEAHGGYTFCALAALAILGKPDKLDlESL----LRWLV 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  250 HRQvsshgcMKFEselnasydqsddGGFQGRENKFADTCYAFW---CLNSLHLLTKDWKMLCQTELVTN--------YLL 318
Cdd:cd02893 205 ARQ------MRFE------------GGFQGRTNKLVDGCYSFWvggSLPILEAILNAEKKFDDSAEGTLfdqealqeYIL 266

                       330       340       350
                ....*....|....*....|....*....|....
gi 6321283  319 DRTQKTlTGGFSKNDEEDADLYHSCLGSAALALI 352
Cdd:cd02893 267 LCCQSE-EGGLRDKPGKPRDFYHTCYALSGLSIA 299
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 38-352 4.54e-27

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: 108.51  E-value: 4.54e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   38 RMAIIFYSISGLSIFDVNVSAKYGDHLgwmrkHYIKTVLDDTentvISGFVGslvmNIPHatTINLPNTLFALLSMIMLR 117
Cdd:cd02894  29 RMSGIYWGLTALDLLGQLERLNREEII-----EFVKSCQDNE----DGGFGG----SPGH--DPHILSTLSAIQILALYD 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  118 DYEYFETILDKrsLARFVSKCQRPDrGSFvscldyktnCGSSVDSDDLRFCYIAVAILYICGcrsKEDfdeYIDTEKLLG 197
Cdd:cd02894  94 LLNKIDENKEK--IAKFIKGLQNED-GSF---------SGDKWGEVDTRFSYCAVLCLTLLG---KLD---LIDVDKAVD 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  198 YIMSqqCYN--GAFGAH--NEPHSGYTSCALSTLALLSsleKLSDKFKEDTITWLLHRQVSShgcmkfeselnasydqsd 273
Cdd:cd02894 156 YLLS--CYNfdGGFGCRpgAESHAGQIFCCVGALAILG---SLDLIDRDRLGWWLCERQLPS------------------ 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  274 dGGFQGRENKFADTCYAFWCLNSLHLLTK-DWkmlCQTELVTNYLLDrTQKTLTGGFSKNDEEDADLYHSCLGSAALALI 352
Cdd:cd02894 213 -GGLNGRPEKLPDVCYSWWVLSSLKIIGRlHW---INKNKLKNFILA-CQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 125-353 9.99e-19

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 85.90  E-value: 9.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   125 ILDKRSLARFVSKCQRPDrGSFVscldyktncGSSVDSDDLRFCYIAVAILYICGCRSKedfdeyIDTEKLLGYIMSQQC 204
Cdd:PLN03201 103 LLDADKVASYVAGLQNED-GSFS---------GDEWGEIDTRFSYCALCCLSLLKRLDK------INVEKAVDYIVSCKN 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   205 YNGAFGAH--NEPHSGYTSCALSTLALLSSLEKLsDKfkeDTITW-LLHRQVSShgcmkfeselnasydqsddGGFQGRE 281
Cdd:PLN03201 167 FDGGFGCTpgGESHAGQIFCCVGALAITGSLHHV-DK---DLLGWwLCERQVKS-------------------GGLNGRP 223

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321283   282 NKFADTCYAFWCLNSLHLLTK-DWkmlCQTELVTNYLLDrTQKTLTGGFSKNDEEDADLYHSCLGSAALALIE 353
Cdd:PLN03201 224 EKLPDVCYSWWVLSSLIIIDRvHW---IDKDKLAKFILD-CQDDENGGISDRPDDAVDVFHTFFGVAGLSLLG 292
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 164-302 1.65e-09

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 59.03  E-value: 1.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283   164 DLRFCYIAVAILYICGCRSKEDfdeyidTEKLLGYIMSQQCYNGAFGAH--NEPHSGYTSCALSTLALLSSLEKLSdkfK 241
Cdd:PLN02710 171 DVRACYTAISVASLLNILDDEL------VKGVGDYILSCQTYEGGIGGEpgAEAHGGYTFCGLAAMILINEVDRLD---L 241

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6321283   242 EDTITWLLHRQvsshgcmkfeselnasydqSDDGGFQGRENKFADTCYAFWCLNSLHLLTK 302
Cdd:PLN02710 242 PSLINWVVFRQ-------------------GVEGGFQGRTNKLVDGCYSFWQGGVFALLQQ 283
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
271-300 5.60e-07

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 45.58  E-value: 5.60e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 6321283    271 QSDDGGFQGRENKFADTCYAFWCLNSLHLL 300
Cdd:pfam00432  14 QNEDGGFGGRPGGESDTYYTYCALAALALL 43
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
127-179 2.33e-04

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 38.26  E-value: 2.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6321283    127 DKRSLARFVSKCQRPDrGSFvscldyktnCGSSVDSDDLRFCYIAVAILYICG 179
Cdd:pfam00432   2 DKEKLVDYLLSCQNED-GGF---------GGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
311-353 3.07e-04

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 37.88  E-value: 3.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 6321283    311 ELVTNYLLDRTQKTltGGFSKNDEEDADLYHSCLGSAALALIE 353
Cdd:pfam00432   4 EKLVDYLLSCQNED--GGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
190-222 2.31e-03

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 35.56  E-value: 2.31e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 6321283    190 IDTEKLLGYIMSQQCYNGAFGAH--NEPHSGYTSC 222
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRpgGESDTYYTYC 35
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
124-351 2.61e-03

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 39.32  E-value: 2.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  124 TILDKRSLARFVSKCQRPDrGSFvscldyktnCGSSVDSDDLRFCYIAVAILYICGcrskEDFDeyiDTEKLLGYIMSQQ 203
Cdd:COG1689   4 LRFDLARTIEYVLKRQNED-GGF---------CAYPGLPSTLADTYYAVRILKLLG----EEVP---NRDKTIEFLESCQ 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  204 CYNGAFGAHNEPHSGYtSCALSTLALLSSLEKLSDKFKEDT------------ITWLLHRQVSSHGCMKFESELNASY-- 269
Cdd:COG1689  67 DEEGGGFALYTTSYGL-MALALLGIDPPDEQEALEYLSDALptkfaggasdleETYLAVALLEALGASEPEREKIREFll 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321283  270 -DQSDDGGFQGRENKFADTCYAFWCLNSLHLLTKDwkmlcQTELVtNYLLDRtQKTlTGGFSKNDEEDADLYHSCLGSAA 348
Cdd:COG1689 146 sLRRPDGGFGGKKPNLEDTYWALAALRRLGRDLPP-----ADRVI-AFILAC-QNE-DGGFSKTPGSYSDLEATYYALRA 217


                ...
gi 6321283  349 LAL 351
Cdd:COG1689 218 LKL 220
 
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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