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Conserved domains on  [gi|392892309|ref|NP_001254400|]
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Geranylgeranyl transferase type I subunit beta [Caenorhabditis elegans]

Protein Classification

prenyltransferase/squalene oxidase repeat-containing protein( domain architecture ID 693)

prenyltransferase/squalene oxidase repeat-containing protein similar to Streptomyces anulatus copalyl diphosphate synthase and Aspergillus fumigatus squalene hopane cyclase afumA

CATH:  1.50.10.20
EC:  5.-.-.-
Gene Ontology:  GO:0016853
SCOP:  3001024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ISOPREN_C2_like super family cl08267
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 1-167 1.16e-83

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.


The actual alignment was detected with superfamily member cd02895:

Pssm-ID: 415487 [Multi-domain]  Cd Length: 307  Bit Score: 249.89  E-value: 1.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAISHILDGDKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTeevLTRRDIDR 80
Cdd:cd02895  144 MRFCYCAVAICYMLDDWSEEDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE---LSEKFLER 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  81 LIRWAIQKQD--IGFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYpePGGYSDILHTY 158
Cdd:cd02895  221 LKRWLVHRQVsgTGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKN--PDSHPDPLHSY 298


                 ....*....
gi 392892309 159 FSIAALSLL 167
Cdd:cd02895  299 LGLAALSLI 307
 
Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 1-167 1.16e-83

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: 249.89  E-value: 1.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAISHILDGDKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTeevLTRRDIDR 80
Cdd:cd02895  144 MRFCYCAVAICYMLDDWSEEDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE---LSEKFLER 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  81 LIRWAIQKQD--IGFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYpePGGYSDILHTY 158
Cdd:cd02895  221 LKRWLVHRQVsgTGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKN--PDSHPDPLHSY 298


                 ....*....
gi 392892309 159 FSIAALSLL 167
Cdd:cd02895  299 LGLAALSLI 307
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 2-189 1.52e-33

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 121.34  E-value: 1.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   2 RFVFCAVAISHILDgdKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRlwteevLTRRDIDRL 81
Cdd:PLN03201 134 RFSYCALCCLSLLK--RLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGS------LHHVDKDLL 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  82 IRWAIQKQ--DIGFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYPEPGgySDILHTYF 159
Cdd:PLN03201 206 GWWLCERQvkSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDA--VDVFHTFF 283

                        170       180       190
                 ....*....|....*....|....*....|
gi 392892309 160 SIAALSLLGEPAVNPVHPSLNVSMRVAERI 189
Cdd:PLN03201 284 GVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 25-174 8.75e-13

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 64.73  E-value: 8.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  25 TKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTEEvltrrdIDRLIRW--AIQKQDIGFHGRAHKPD- 101
Cdd:COG5029  116 DRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPI------ETKVIRFlrDVQSPEGGFAYNTRIGEa 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392892309 102 DSCYAFWIGATLKILNAYHLVsKQHLREFLMICQHPhIGGFcKYPEPGGYSDILHTYFSIAALSLLGEPAVNP 174
Cdd:COG5029  190 DLLSTFTAILTLYDLGAAPKL-VDDLQAYILSLQLP-DGGF-EGAPWDGVEDVEYTFYGVGALALLGALAERG 259
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
127-168 4.60e-07

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 44.81  E-value: 4.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 392892309  127 LREFLMICQHPHiGGFCKYPepGGYSDILHTYFSIAALSLLG 168
Cdd:pfam00432   6 LVDYLLSCQNED-GGFGGRP--GGESDTYYTYCALAALALLG 44
 
Name Accession Description Interval E-value
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 1-167 1.16e-83

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: 249.89  E-value: 1.16e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAISHILDGDKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTeevLTRRDIDR 80
Cdd:cd02895  144 MRFCYCAVAICYMLDDWSEEDIDKEKLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEE---LSEKFLER 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  81 LIRWAIQKQD--IGFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYpePGGYSDILHTY 158
Cdd:cd02895  221 LKRWLVHRQVsgTGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKN--PDSHPDPLHSY 298


                 ....*....
gi 392892309 159 FSIAALSLL 167
Cdd:cd02895  299 LGLAALSLI 307
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 1-167 4.92e-70

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: 214.37  E-value: 4.92e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAISHILDGDKEqtIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLwteevlTRRDIDR 80
Cdd:cd02890  127 TRFVYCALSILSLLNILTD--IDKEKLIDYILSCQNYDGGFGGVPGAESHGGYTFCAVASLALLGRL------DLIDKER 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  81 LIRWAIQKQDI---GFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKypEPGGYSDILHT 157
Cdd:cd02890  199 LLRWLVERQLAsggGFNGRPNKLVDTCYSFWVGASLKILGRLHLIDQEKLREYILSCQQSEVGGFSD--KPGKPPDLYHT 276

                        170
                 ....*....|
gi 392892309 158 YFSIAALSLL 167
Cdd:cd02890  277 YYGLSGLSLL 286
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 1-167 1.49e-48

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: 159.36  E-value: 1.49e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAISHILDgdKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRlwteevLTRRDIDR 80
Cdd:cd02894  129 TRFSYCAVLCLTLLG--KLDLIDVDKAVDYLLSCYNFDGGFGCRPGAESHAGQIFCCVGALAILGS------LDLIDRDR 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  81 LIRWAIQKQDI--GFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKypEPGGYSDILHTY 158
Cdd:cd02894  201 LGWWLCERQLPsgGLNGRPEKLPDVCYSWWVLSSLKIIGRLHWINKNKLKNFILACQDEEDGGFAD--RPGNMVDVFHTF 278


                 ....*....
gi 392892309 159 FSIAALSLL 167
Cdd:cd02894  279 FGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 2-189 1.52e-33

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 121.34  E-value: 1.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   2 RFVFCAVAISHILDgdKEQTIDWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRlwteevLTRRDIDRL 81
Cdd:PLN03201 134 RFSYCALCCLSLLK--RLDKINVEKAVDYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALAITGS------LHHVDKDLL 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  82 IRWAIQKQ--DIGFHGRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYPEPGgySDILHTYF 159
Cdd:PLN03201 206 GWWLCERQvkSGGLNGRPEKLPDVCYSWWVLSSLIIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDA--VDVFHTFF 283

                        170       180       190
                 ....*....|....*....|....*....|
gi 392892309 160 SIAALSLLGEPAVNPVHPSLNVSMRVAERI 189
Cdd:PLN03201 284 GVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 1-166 6.31e-31

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: 114.25  E-value: 6.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAIS---HILDGD-KEQTIDWtklagfLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRlwteevLTRR 76
Cdd:cd02893  127 VRGTYCAISVAsllNILTDElFEGVAEY------ILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILGK------PDKL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  77 DIDRLIRWAIQKQDI---GFHGRAHKPDDSCYAFWIGATLKILNAYH-------------LVSKQHLREFLMICQHPHIG 140
Cdd:cd02893  195 DLESLLRWLVARQMRfegGFQGRTNKLVDGCYSFWVGGSLPILEAILnaekkfddsaegtLFDQEALQEYILLCCQSEEG 274

                        170       180
                 ....*....|....*....|....*.
gi 392892309 141 GFcKYpEPGGYSDILHTYFSIAALSL 166
Cdd:cd02893  275 GL-RD-KPGKPRDFYHTCYALSGLSI 298
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 1-167 4.43e-29

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: 109.18  E-value: 4.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   1 MRFVFCAVAISHILdGDKEQTIDWTKLAGFLRQSLNIDGGIGqaPGDESHGGSTFCAIASLALSNRlwteevLTRRDIDR 80
Cdd:cd00688  140 VRLTAYALIALALL-GKLDPDPLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGD------LDSPDAKK 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  81 LIRWAIQKQDIGFHG-----RAHKPDDSCYAFWIGATLKILNAY-HLVSKQHLREFLMICQHPHiGGFckYPEPGGYSDI 154
Cdd:cd00688  211 ALRWLLSRQRPDGGWgegrdRTNKLSDSCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQNED-GGF--SSKPGKSYDT 287

                        170
                 ....*....|...
gi 392892309 155 LHTYFSIAALSLL 167
Cdd:cd00688  288 QHTVFALLALSLY 300
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 6-143 4.63e-17

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 78.29  E-value: 4.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   6 CAVAIS-----HILDGDKEQtidwtKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNrlwteEVlTRRDIDR 80
Cdd:PLN02710 175 CYTAISvasllNILDDELVK-----GVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILIN-----EV-DRLDLPS 243

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392892309  81 LIRWAIQKQDI--GFHGRAHKPDDSCYAFWIGATLKILNAYH-LVSKQHLREFLMICQHPHIGGFC 143
Cdd:PLN02710 244 LINWVVFRQGVegGFQGRTNKLVDGCYSFWQGGVFALLQQLVtIVDEQLQTGGSSIMFEELEDDAC 309
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 25-174 8.75e-13

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 64.73  E-value: 8.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  25 TKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTEEvltrrdIDRLIRW--AIQKQDIGFHGRAHKPD- 101
Cdd:COG5029  116 DRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPI------ETKVIRFlrDVQSPEGGFAYNTRIGEa 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392892309 102 DSCYAFWIGATLKILNAYHLVsKQHLREFLMICQHPhIGGFcKYPEPGGYSDILHTYFSIAALSLLGEPAVNP 174
Cdd:COG5029  190 DLLSTFTAILTLYDLGAAPKL-VDDLQAYILSLQLP-DGGF-EGAPWDGVEDVEYTFYGVGALALLGALAERG 259
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 104-175 2.34e-10

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: 58.36  E-value: 2.34e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392892309 104 CYAFWIGATLKILNAYHLVS-KQHLREFLMICQHPHIGGFCkyPEPGGYSDILHTYFSIAALSLLGEPAVNPV 175
Cdd:cd02890   28 WLLYWILSSLDLLGEDLDDEnKDEIIDFIYSCQVNEDGGFG--GGPGQDPHLASTYAAVLSLAILGDDALSRI 98
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 22-170 4.52e-09

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: 54.48  E-value: 4.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  22 IDWTKLAGFLRQSLNIDGG-------IGQAPGDESHGGSTFCAIASLALSNRLWTEEvltrrDIDRLIRWAIQKQDIGFH 94
Cdd:cd00688  104 IDLARALNWLLSLQNEDGGfredgpgNHRIGGDESDVRLTAYALIALALLGKLDPDP-----LIEKALDYLLSCQNYDGG 178

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 392892309  95 GRAHKPDDSCYAFWIGATLKILNAYHLVSKQHLREFLMICQHPHIGGFCKYPEPGGYSDILHTYFSIAALSLLGEP 170
Cdd:cd00688  179 FGPGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDRTNKLSDSCYTEWAAYALLALGKL 254
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
127-168 4.60e-07

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 44.81  E-value: 4.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 392892309  127 LREFLMICQHPHiGGFCKYPepGGYSDILHTYFSIAALSLLG 168
Cdd:pfam00432   6 LVDYLLSCQNED-GGFGGRP--GGESDTYYTYCALAALALLG 44
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
4-170 5.30e-07

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 48.57  E-value: 5.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309   4 VFCAVAISHILDGDKEQTIDWTKlagFLRQSLNIDGGIGqapGDESHGGSTFCAIASLALSNRlwteevlTRRDIDRLIR 83
Cdd:COG1689  120 TYLAVALLEALGASEPEREKIRE---FLLSLRRPDGGFG---GKKPNLEDTYWALAALRRLGR-------DLPPADRVIA 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  84 W--AIQKQDIGFhgrAHKPDDSCYA---FWIGATLKILNA-YHLVSKqhLREFLMICQHPHiGGFCKYPEpGGYSDILHT 157
Cdd:COG1689  187 FilACQNEDGGF---SKTPGSYSDLeatYYALRALKLLGEpPKNVDK--LLEFIASCQNSD-GGFRRSPE-GGISTLEYT 259

                        170
                 ....*....|...
gi 392892309 158 YFSIAALSLLGEP 170
Cdd:COG1689  260 YYALAVLKWLKRL 272
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 26-169 6.65e-07

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 48.16  E-value: 6.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  26 KLAGFLRQSLNIDGGIGQAPgdESHGGSTFCAIASLALSnrlwteEVLTR--RDIDRLIRWAIQKQ--DIGFHGRA-HKP 100
Cdd:COG5029   69 RVADLLSSLRVEDGGFAKAP--EGGAGSTYHTYLATLLA------ELLGRppPDPDRLVRFLISQQndDGGFEISPgRRS 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392892309 101 DDSCYAFWIGAtLKILNAYHLVSKQHLREFLMICQHPHiGGFcKYPEPGGYSDILHTYFSIAALSLLGE 169
Cdd:COG5029  141 DTNPTAAAIGA-LRALGALDDPIETKVIRFLRDVQSPE-GGF-AYNTRIGEADLLSTFTAILTLYDLGA 206
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
26-63 1.01e-05

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 40.96  E-value: 1.01e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 392892309   26 KLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLAL 63
Cdd:pfam00432   5 KLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 27-169 1.34e-05

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 44.31  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  27 LAGFLRQSLNIDGGIGQAPGdESHGGSTFCAIASLALSNrlwtEEVLTRRDIDRLIRwAIQKQDIGF-HGRAHKPDDSCY 105
Cdd:COG5029   24 HLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLG----ESPKWRDRVADLLS-SLRVEDGGFaKAPEGGAGSTYH 97

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392892309 106 AFWIGATLKILNaYHLVSKQHLREFLMICQHPHiGGFcKYPePGGYSDILHTYFSIAALSLLGE 169
Cdd:COG5029   98 TYLATLLAELLG-RPPPDPDRLVRFLISQQNDD-GGF-EIS-PGRRSDTNPTAAAIGALRALGA 157
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
23-193 1.45e-05

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 44.33  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  23 DWTKLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLalsnRLWTEEVLTRrdiDRLIRW--AIQKQDIGFHG----- 95
Cdd:COG1689    7 DLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRIL----KLLGEEVPNR---DKTIEFleSCQDEEGGGFAlytts 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  96 ---------------------RAHKPDDSCYA---------FWIGATLKIL----------------------------- 116
Cdd:COG1689   80 yglmalallgidppdeqealeYLSDALPTKFAggasdleetYLAVALLEALgaseperekirefllslrrpdggfggkkp 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309 117 ---NAYHLVS-----------KQHLREFLMICQHPHiGGFCKypEPGGYSDILHTYFSIAALSLLGEPAVNPvhpslnvs 182
Cdd:COG1689  160 nleDTYWALAalrrlgrdlppADRVIAFILACQNED-GGFSK--TPGSYSDLEATYYALRALKLLGEPPKNV-------- 228

                        250
                 ....*....|.
gi 392892309 183 MRVAERIARLQ 193
Cdd:COG1689  229 DKLLEFIASCQ 239
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 13-173 1.77e-05

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: 44.11  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  13 ILDGDKEQTIDWTKlagflRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRlwteEVLTRRDIDRLIRWaiqkqdig 92
Cdd:cd02890   44 LDDENKDEIIDFIY-----SCQVNEDGGFGGGPGQDPHLASTYAAVLSLAILGD----DALSRIDREKIYKF-------- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  93 fhgrahkpddscyafwigatlkilnayhlvskqhlrefLMICQHPHiGGFCkyPEPGGYSDILHTYFSIAALSLLGEPAV 172
Cdd:cd02890  107 --------------------------------------LSSLQNPD-GSFR--GDLGGEVDTRFVYCALSILSLLNILTD 145


                 .
gi 392892309 173 N 173
Cdd:cd02890  146 I 146
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 26-175 3.54e-04

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: 40.23  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  26 KLAGFLRQSLNIDGGIGQAPGDESHGGSTFCAIASLALSNRLWTEEvLTRRDIDRLIRW--AIQKQDIGF-----HGRAH 98
Cdd:cd00688    3 KHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAATGIRD-KADENIEKGIQRllSYQLSDGGFsgwggNDYPS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392892309  99 kPDDSCYAFWIgatLKILNAYHLVSKQHLR---EFLMICQHPhIGGFCKY-----PEPGGYSDILHTYFSIAALSLLGEP 170
Cdd:cd00688   82 -LWLTAYALKA---LLLAGDYIAVDRIDLAralNWLLSLQNE-DGGFREDgpgnhRIGGDESDVRLTAYALIALALLGKL 156


                 ....*
gi 392892309 171 AVNPV 175
Cdd:cd00688  157 DPDPL 161
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 125-193 1.34e-03

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 38.53  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392892309 125 QHLREFLMICQHPHiGGFckyPEPGGYSDILHTYFSIAALSLLGEPavnPVHPSlnvsmRVAERIARLQ 193
Cdd:COG5029   22 DSHLDYLRASQNPD-GGF---AGRSGPSDLYSTYYAVRTLALLGES---PKWRD-----RVADLLSSLR 78
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
77-117 1.69e-03

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 35.18  E-value: 1.69e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 392892309   77 DIDRLIRW--AIQKQDIGFHGRAHKPDDSCYAFWIGATLKILN 117
Cdd:pfam00432   2 DKEKLVDYllSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
 
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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