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Conserved domains on  [gi|542206677|ref|XP_005476758|]
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geranylgeranyl transferase type-2 subunit beta [Oreochromis niloticus]

Protein Classification

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

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

CATH:  1.50.10.20
EC:  2.5.1.60
Gene Ontology:  GO:0004663|GO:0018344|GO:0005968|GO:0031267|GO:0008270
PubMed:  8621375
SCOP:  4001193

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 18-301 0e+00

Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.


:

Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 538.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  18 LLLEKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLPRMNQQEIIDFIKACQ-HECGGISASIGHDPHLL 96
Cdd:cd02894    1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  97 YTLSAVQILCLYDSIDAID--VDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLSC 174
Cdd:cd02894   81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 175 MNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894  161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 542206677 255 IRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02894  241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 18-301 0e+00

Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.


Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 538.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  18 LLLEKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLPRMNQQEIIDFIKACQ-HECGGISASIGHDPHLL 96
Cdd:cd02894    1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  97 YTLSAVQILCLYDSIDAID--VDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLSC 174
Cdd:cd02894   81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 175 MNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894  161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 542206677 255 IRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02894  241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-326 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 515.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  14 APSTLLLEKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLPRMNQQEIIDFIKACQHECGGISASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  94 HLLYTLSAVQILCLYDSIDAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 174 CMNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542206677 254 RIRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLLGDEQIKPVNPVLCMPEDVLQRIGLQ 326
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 73-302 4.10e-31

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 117.88  E-value: 4.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  73 DFIKACQHECGGISASIGhDPHLLYTLSAVQILCLYDSIDAIDvDKVVEYVKGLQQEDGSFA-GDKWGEIDTRFSFCAVA 151
Cdd:COG5029   26 DYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkAPEGGAGSTYHTYLATL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 152 TLALLGkMDTINVDKAVEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNG 231
Cdd:COG5029  104 LAELLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAY 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542206677 232 RPEK-LPDVCYSWWVLASLKIIGrIRWIDKDKLRKFILACQDEEtGGFADRPGDMV-DPFHTLFGVAGLSLLG 302
Cdd:COG5029  183 NTRIgEADLLSTFTAILTLYDLG-AAPKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
114-157 2.57e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.60  E-value: 2.57e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 542206677  114 IDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLG 157
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 5.29e-05

squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.


Pssm-ID: 273809 [Multi-domain]  Cd Length: 621  Bit Score: 44.74  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677   98 TLSAVQILCLY----DSIDAIdVDKVVEYVKGLQQEDGSFAGdKWGEIDTRFSFCAVATLALLGKM--DTINVDKAVEFV 171
Cdd:TIGR01787 441 TARVIQALGAFghraDEIRNV-LERALEYLRREQRADGSWFG-RWGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWL 518

                          90
                  ....*....|.
gi 542206677  172 LSCMNFDGGFG 182
Cdd:TIGR01787 519 LSRQMPDGGWG 529
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 18-301 0e+00

Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). GGTase-IIs are a subgroup of the protein prenyltransferase family of lipid-modifying enzymes. PTases catalyze the carboxyl-terminal lipidation of Ras, Rab, and several other cellular signal transduction proteins, facilitating membrane associations and specific protein-protein interactions. Prenyltransferases employ a Zn2+ ion to alkylate a thiol group catalyzing the formation of thioether linkages between cysteine residues at or near the C-terminus of protein acceptors and the C1 atom of isoprenoid lipids (geranylgeranyl (20-carbon) in the case of GGTase-II ). GGTase-II catalyzes alkylation of both cysteine residues in Rab proteins containing carboxy-terminal "CC", "CXCX" or "CXC" motifs. PTases are heterodimeric with both alpha and beta subunits required for catalytic activity. In contrast to other prenyltransferases, GGTas-II requires an escort protein to bring the substrate protein to the catalytic heterodimer and to escort the geryanylgeranylated product to the membrane.


Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 538.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  18 LLLEKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLPRMNQQEIIDFIKACQ-HECGGISASIGHDPHLL 96
Cdd:cd02894    1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  97 YTLSAVQILCLYDSIDAID--VDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLSC 174
Cdd:cd02894   81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 175 MNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894  161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 542206677 255 IRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02894  241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-326 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 515.79  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  14 APSTLLLEKHADYIAAYGSKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQLPRMNQQEIIDFIKACQHECGGISASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  94 HLLYTLSAVQILCLYDSIDAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 174 CMNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542206677 254 RIRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLLGDEQIKPVNPVLCMPEDVLQRIGLQ 326
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRIGLR 316
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 20-301 7.63e-149

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: 420.07  E-value: 7.63e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  20 LEKHADYIAAYGsKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQ-LPRMNQQEIIDFIKACQ-HECGGISASIGHDPHLLY 97
Cdd:cd02890    1 REKHIKYLQRCL-KLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHLAS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  98 TLSAVQILCLYDS--IDAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLSCM 175
Cdd:cd02890   80 TYAAVLSLAILGDdaLSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 176 NFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSG-GLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02890  160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKILGR 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 542206677 255 IRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02890  240 LHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 20-301 4.10e-78

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: 240.92  E-value: 4.10e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  20 LEKHADYIAAYGsKKDDYEYTLSEYLRMSGIYWGLTVMDLMGQ------LPRMNQQEIIDFIKACQHECGGISASIGHD- 92
Cdd:cd00688    1 IEKHLKYLLRYP-YGDGHWYQSLCGEQTWSTAWPLLALLLLLAatgirdKADENIEKGIQRLLSYQLSDGGFSGWGGNDy 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  93 PHLLYTLSAVQILCL---YDSIDAIDVDKVVEYVKGLQQEDGSFAGDKWG-------EIDTRFSFCAVATLALLGKMDT- 161
Cdd:cd00688   80 PSLWLTAYALKALLLagdYIAVDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDPd 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 162 INVDKAVEFVLSCMNFDGGFGcrPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNGRPE---KLPD 238
Cdd:cd00688  160 PLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnKLSD 237

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 542206677 239 VCYSWWVLASLKIIGRIR-WIDKDKLRKFILACQDeETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd00688  238 SCYTEWAAYALLALGKLGdLEDAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 46-301 4.92e-71

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: 222.92  E-value: 4.92e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  46 RMSGIYWGLTVMDLMGQL---PRMNQQEIIDFIKACQ----HECGGISASIGHD----------PHLLYTLSAVQIL-CL 107
Cdd:cd02895   26 RLTIAFFALSGLDLLGALdsiLVEEKDDIIEWIYSLQvlsnLPRGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLlIL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 108 YDSIDAIDVDKVVEYVKGLQQEDGSFAGDKW---GEIDTRFSFCAVATLALLG--KMDTINVDKAVEFVLSCMNFDGGFG 182
Cdd:cd02895  106 GDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYMLDdwSEEDIDKEKLIDYIKSSQSYDGGFG 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 183 CRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGW---WLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRIRWID 259
Cdd:cd02895  186 QGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERlkrWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLID 265

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 542206677 260 KDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLL 301
Cdd:cd02895  266 FEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 50-300 4.11e-66

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: 210.17  E-value: 4.11e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  50 IYWGLTVMDLMG-QLPRMNQQEIIDFIKACQHECGGISASIGHDPHLLYTLSAVQILCLYDSIDA---IDVDKVVEYVKG 125
Cdd:cd02893   30 LYWILHSLELLGeELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTYAAVNALAIIGTEEAydvIDREALYKFLLS 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 126 LQQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLSLTG 205
Cdd:cd02893  110 LKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILG 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 206 QLHQLNADLLGWWLCERQLPS-GGLNGRPEKLPDVCYSWWVLASLKIIGRI-------------RWIDKDKLRKFILACQ 271
Cdd:cd02893  190 KPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPILEAIlnaekkfddsaegTLFDQEALQEYILLCC 269

                        250       260
                 ....*....|....*....|....*....
gi 542206677 272 DEETGGFADRPGDMVDPFHTLFGVAGLSL 300
Cdd:cd02893  270 QSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 51-299 4.41e-34

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 129.52  E-value: 4.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  51 YWGLTVMDLMGQ-LPRMNQQEIIDFIKACQHECGGISASIGHDPHLLYTLSAVQILCLYDS---IDAIDVDKVVEYVKGL 126
Cdd:PLN02710  76 YWILHSIALLGEsLDDELENDTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLVTIGGeraLSSINREKLYTFLLRM 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 127 QQEDGSFAGDKWGEIDTRFSFCAVATLALLGKMDTINVDKAVEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQ 206
Cdd:PLN02710 156 KDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINE 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 207 LHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRIRWIDKDK------------------------ 262
Cdd:PLN02710 236 VDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFALLQQLVTIVDEQlqtggssimfeeleddacetsssg 315

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542206677 263 -----------------------------------LRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLS 299
Cdd:PLN02710 316 kddagdtdsadyskvgfdfikasnqqmgplfhsiaLQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLS 387
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 73-302 4.10e-31

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 117.88  E-value: 4.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  73 DFIKACQHECGGISASIGhDPHLLYTLSAVQILCLYDSIDAIDvDKVVEYVKGLQQEDGSFA-GDKWGEIDTRFSFCAVA 151
Cdd:COG5029   26 DYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkAPEGGAGSTYHTYLATL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 152 TLALLGkMDTINVDKAVEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQLNADLLGWWLCERQLPSGGLNG 231
Cdd:COG5029  104 LAELLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAY 182

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542206677 232 RPEK-LPDVCYSWWVLASLKIIGrIRWIDKDKLRKFILACQDEEtGGFADRPGDMV-DPFHTLFGVAGLSLLG 302
Cdd:COG5029  183 NTRIgEADLLSTFTAILTLYDLG-AAPKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGALALLG 253
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 14-254 4.44e-21

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 90.54  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  14 APSTLLLEKHADYIAA-------YG--SKKDDYEYTlseylrmsgiYWGLTVMDLMGQLPRmNQQEIIDFIKACQHECGG 84
Cdd:COG5029   15 KSTADFTDSHLDYLRAsqnpdggFAgrSGPSDLYST----------YYAVRTLALLGESPK-WRDRVADLLSSLRVEDGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  85 -------ISASIGHdpHLLYTLSAVqilcLYDsIDAIDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLG 157
Cdd:COG5029   84 fakapegGAGSTYH--TYLATLLAE----LLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 158 KMDTINVDKAVEFVLSCMNFDGGFGCRPgSESHAGQIYCCTGFLSltgqLHQLNA-----DLLGWWLCERQLPSGGLNGR 232
Cdd:COG5029  157 ALDDPIETKVIRFLRDVQSPEGGFAYNT-RIGEADLLSTFTAILT----LYDLGAapklvDDLQAYILSLQLPDGGFEGA 231

                        250       260
                 ....*....|....*....|...
gi 542206677 233 P-EKLPDVCYSWWVLASLKIIGR 254
Cdd:COG5029  232 PwDGVEDVEYTFYGVGALALLGA 254
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
64-303 3.01e-20

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 88.63  E-value: 3.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  64 PRMNQQEIIDFIKACQHECGGISASIGHDPHLLYTLSAVQIL-CLYDSIDaiDVDKVVEYVKGLQQEDGSFAG------- 135
Cdd:COG1689    4 LRFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILkLLGEEVP--NRDKTIEFLESCQDEEGGGFAlyttsyg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 136 ----------------------------DKWGEIDTRFSFCAVATLALLGKmDTINVDKAVEFVLSCMNFDGGFGcrpGS 187
Cdd:COG1689   82 lmalallgidppdeqealeylsdalptkFAGGASDLEETYLAVALLEALGA-SEPEREKIREFLLSLRRPDGGFG---GK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 188 ESHAGQIYCCTGFLSLTGQlHQLNADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRiRWIDKDKLRKFI 267
Cdd:COG1689  158 KPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQNEDGGFSKTPGSYSDLEATYYALRALKLLGE-PPKNVDKLLEFI 235

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 542206677 268 LACQdEETGGFADRPGDMV-DPFHTLFGVAGLSLLGD 303
Cdd:COG1689  236 ASCQ-NSDGGFRRSPEGGIsTLEYTYYALAVLKWLKR 271
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
50-254 9.24e-17

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 79.00  E-value: 9.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  50 IYWGLTVMDLMGQLPRMNQQEIIDFIKACQHECGGISASIghdpHLLYTLSAvqiLCLYDSIDAIDVDKVVEYVKGLQQE 129
Cdd:COG1689   78 TSYGLMALALLGIDPPDEQEALEYLSDALPTKFAGGASDL----EETYLAVA---LLEALGASEPEREKIREFLLSLRRP 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 130 DGSFAGDKWGEIDTRFsfcAVATLALLGkMDTINVDKAVEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLSLTGQLHQ 209
Cdd:COG1689  151 DGGFGGKKPNLEDTYW---ALAALRRLG-RDLPPADRVIAFILACQNEDGGFSKTPGSYSDLEATYYALRALKLLGEPPK 226

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 542206677 210 LNADLLgWWLCERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGR 254
Cdd:COG1689  227 NVDKLL-EFIASCQNSDGGFRRSPEGgISTLEYTYYALAVLKWLKR 271
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 165-303 2.21e-12

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 65.88  E-value: 2.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 165 DKAVEFVLSCMNFDGGFGCRPGsESHAGQIYCCTGFLSLTGQLHQLNADLLGWWL-CERqlPSGGLNGRPEKLPDVCY-S 242
Cdd:COG5029   22 DSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRV--EDGGFAKAPEGGAGSTYhT 98

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542206677 243 WWVLASLKIIGRiRWIDKDKLRKFILACQDEEtGGFADRPGDMVDPFHTLFGVAGLSLLGD 303
Cdd:COG5029   99 YLATLLAELLGR-PPPDPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGALRALGA 157
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
114-157 2.57e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.60  E-value: 2.57e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 542206677  114 IDVDKVVEYVKGLQQEDGSFAGDKWGEIDTRFSFCAVATLALLG 157
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
162-205 3.26e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.22  E-value: 3.26e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 542206677  162 INVDKAVEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLSLTG 205
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
211-253 2.86e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.52  E-value: 2.86e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 542206677  211 NADLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:pfam00432   2 DKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
258-302 2.40e-10

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 55.21  E-value: 2.40e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 542206677  258 IDKDKLRKFILACQDEEtGGFADRPGDMVDPFHTLFGVAGLSLLG 302
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
66-109 1.27e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 50.20  E-value: 1.27e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 542206677   66 MNQQEIIDFIKACQHECGGISASIGHDPHLLYTLSAVQILCLYD 109
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 244-315 2.52e-07

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


Pssm-ID: 239220 [Multi-domain]  Cd Length: 286  Bit Score: 51.43  E-value: 2.52e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 542206677 244 WVLASLKIIGR-IRWIDKDKLRKFILACQDEETGGFADRPGDMVDPFHTLFGVAGLSLLGDEQIKPVNPVLCM 315
Cdd:cd02890   32 WILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSLAILGDDALSRIDREKIY 104
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 117-303 1.05e-05

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 46.70  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 117 DKVVEYV-KGLQQEDGSF----AGDKWgeidtrFSFCAVATLALLGK-MDTINVDKAVEFVLSCMNFDGGFGCRPGSESH 190
Cdd:PLN02710  47 EKHLEYLtRGLRQLGPSFsvldANRPW------LCYWILHSIALLGEsLDDELENDTIDFLSRCQDPNGGYGGGPGQLPH 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 191 AGQIYCCTGFLSLTG---QLHQLNADLLGWWLCERQLPSGGLNGRPEKLPDV--CYSWWVLASLKIIgrirwIDK---DK 262
Cdd:PLN02710 121 LATTYAAVNTLVTIGgerALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVraCYTAISVASLLNI-----LDDelvKG 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 542206677 263 LRKFILACQDEEtGGFADRPGDMVDPFHTLFGVAGLSLLGD 303
Cdd:PLN02710 196 VGDYILSCQTYE-GGIGGEPGAEAHGGYTFCGLAAMILINE 235
PLN03012 PLN03012
Camelliol C synthase
 98-182 2.58e-05

Camelliol C synthase


Pssm-ID: 166653 [Multi-domain]  Cd Length: 759  Bit Score: 45.78  E-value: 2.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677  98 TLSAVQILCLY---------DSIDAIdVDKVVEYVKGLQQEDGSFAGDkWGEIDTRFSFCAVATLALLGKM--DTINVDK 166
Cdd:PLN03012 566 TSSAIQALILFkqlypdhrtEEINAF-IKKAAEYIENIQMLDGSWYGN-WGICFTYGTWFALAGLAAAGKTfnDCEAIRK 643

                         90
                 ....*....|....*.
gi 542206677 167 AVEFVLSCMNFDGGFG 182
Cdd:PLN03012 644 GVHFLLAAQKDNGGWG 659
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 5.29e-05

squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the triterpenes squalene or 2-3-oxidosqualene to a variety of products including hopene, lanosterol, cycloartenol, amyrin, lupeol, and isomultiflorenol.


Pssm-ID: 273809 [Multi-domain]  Cd Length: 621  Bit Score: 44.74  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677   98 TLSAVQILCLY----DSIDAIdVDKVVEYVKGLQQEDGSFAGdKWGEIDTRFSFCAVATLALLGKM--DTINVDKAVEFV 171
Cdd:TIGR01787 441 TARVIQALGAFghraDEIRNV-LERALEYLRREQRADGSWFG-RWGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDWL 518

                          90
                  ....*....|.
gi 542206677  172 LSCMNFDGGFG 182
Cdd:TIGR01787 519 LSRQMPDGGWG 529
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 116-182 9.67e-05

Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. Bacterial SQCY catalyzes the convertion of squalene to hopene or diplopterol. Eukaryotic OSQCY transforms the 2,3-epoxide of squalene to compounds such as, lanosterol (a metabolic precursor of cholesterol and steroid hormones) in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain. This group also contains SQCY-like archael sequences and some bacterial SQCY's which lack this minor domain.


Pssm-ID: 239219 [Multi-domain]  Cd Length: 348  Bit Score: 43.75  E-value: 9.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 542206677 116 VDKVVEYVKGLQQEDGSFAGdKWGeID----TRFSFCAvatLALLGKMDTIN-VDKAVEFVLSCMNFDGGFG 182
Cdd:cd02889  193 IRRAVKYLEREQEPDGSWYG-RWG-VCfiygTWFALEA---LAAAGEDENSPyVRKACDWLLSKQNPDGGWG 259
SQCY_1 cd02892
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
 116-227 6.60e-04

Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an alpha 6 - alpha 6 barrel fold. Squalene cyclase (SQCY) and 2,3-oxidosqualene cyclase (OSQCY) are integral membrane proteins that catalyze a cationic cyclization cascade converting linear triterpenes to fused ring compounds. This group contains bacterial SQCY which catalyzes the convertion of squalene to hopene or diplopterol and eukaryotic OSQCY which transforms the 2,3-epoxide of squalene to compounds such as, lanosterol in mammals and fungi or, cycloartenol in plants. Deletion of a single glycine residue of Alicyclobacillus acidocaldarius SQCY alters its substrate specificity into that of eukaryotic OSQCY. Both enzymes have a second minor domain, which forms an alpha-alpha barrel that is inserted into the major domain.


Pssm-ID: 239222 [Multi-domain]  Cd Length: 634  Bit Score: 41.41  E-value: 6.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 542206677 116 VDKVVEYVKGLQQEDGSFAGdKWGEIDTRFSFCAVATLALLGK--MDTINVDKAVEFVLSCMNFDGGFG-----CRPGS- 187
Cdd:cd02892  478 IRRAVKYLLREQEPDGSWYG-RWGVCYIYGTWFALEALAAAGEdyENSPYIRKACDFLLSKQNPDGGWGesylsYEDKSy 556

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 542206677 188 -ESHAGQIyCCTGFlSLTGQLHQLNADLLGW-----WLCERQLPSG 227
Cdd:cd02892  557 aGGGRSTV-VQTAW-ALLALMAAGEPDSEAVergikYLLNTQLPDG 600
PLN02993 PLN02993
lupeol synthase
 116-190 7.34e-04

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 41.44  E-value: 7.34e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 542206677 116 VDKVVEYVKGLQQEDGSFAGDkWGEIDTRFSFCAVATLALLGKM--DTINVDKAVEFVLSCMNFDGGFGcrpgsESH 190
Cdd:PLN02993 592 IEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAGKTynDCLAMRKGVHFLLTIQRDDGGWG-----ESY 662
hopene_cyclase TIGR01507
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ...
 116-182 2.90e-03

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


Pssm-ID: 273661 [Multi-domain]  Cd Length: 635  Bit Score: 39.49  E-value: 2.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 542206677  116 VDKVVEYVKGLQQEDGSFAGdKWGeidTRFSFCAVATLALLGKMDTIN----VDKAVEFVLSCMNFDGGFG 182
Cdd:TIGR01507 473 IERAVEYLKREQEPDGSWFG-RWG---VNYLYGTGAVLSALKAVGIDTrepyIQKALAWLESHQNPDGGWG 539
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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