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Conserved domains on  [gi|1216504|gb|AAA91473|]
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geranylgeranyl transferase type II beta-subunit [Homo sapiens]

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: 548.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   18 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQ-HECGGISASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   97 YTLSAVQILTLYDSINVID--VNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  175 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 1216504  255 LHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 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: 548.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   18 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQ-HECGGISASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   97 YTLSAVQILTLYDSINVID--VNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  175 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 1216504  255 LHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd02894 241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-323 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 517.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    14 APDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    94 HLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   174 CMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   254 RLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVLQRV 323
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 68-302 9.49e-27

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 105.94  E-value: 9.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   68 REEILAFIKSCQHECGGISASIGhDPHLLYTLSAVQILTLYDSINVIDvNKVVEYVKGLQKEDGSFA-------GDIWGe 140
Cdd:COG5029  21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  141 idtrfSFCAVATFALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLC 220
Cdd:COG5029  98 -----TYLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLR 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  221 ERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRNFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGL 298
Cdd:COG5029 172 DVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGAL 249


                ....
gi 1216504  299 SLLG 302
Cdd:COG5029 250 ALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
162-203 1.83e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.99  E-value: 1.83e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1216504    162 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 203
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 3.43e-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: 45.51  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504     98 TLSAVQILTLY----DSI-NVIdvNKVVEYVKGLQKEDGSFAGDiWGEIDTRFSFCAVATFALLGKL--DAINVEKAIEF 170
Cdd:TIGR01787 441 TARVIQALGAFghraDEIrNVL--ERALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDW 517

                          90
                  ....*....|..
gi 1216504    171 VLSCMNFDGGFG 182
Cdd:TIGR01787 518 LLSRQMPDGGWG 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: 548.02  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   18 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQ-HECGGISASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   97 YTLSAVQILTLYDSINVID--VNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIDenKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  175 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 1216504  255 LHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd02894 241 LHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 14-323 0e+00

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 517.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    14 APDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    94 HLLYTLSAVQILTLYDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   174 CMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   254 RLHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVNPVFCMPEEVLQRV 323
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 20-301 1.74e-147

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: 416.60  E-value: 1.74e-147
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   20 LEKHADYIASYGsKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQ-LHRMNREEILAFIKSCQ-HECGGISASIGHDPHLLY 97
Cdd:cd02890   1 REKHIKYLQRCL-KLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHLAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   98 TLSAVQILTLYDS--INVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLSCM 175
Cdd:cd02890  80 TYAAVLSLAILGDdaLSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  176 NFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSG-GLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02890 160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKILGR 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 1216504  255 LHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd02890 240 LHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 20-301 7.89e-79

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: 242.84  E-value: 7.89e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   20 LEKHADYIASYGsKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLH------RMNREEILAFIKSCQHECGGISASIGHD- 92
Cdd:cd00688   1 IEKHLKYLLRYP-YGDGHWYQSLCGEQTWSTAWPLLALLLLLAATgirdkaDENIEKGIQRLLSYQLSDGGFSGWGGNDy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   93 PHLLYTLSAVQILTL---YDSINVIDVNKVVEYVKGLQKEDGSFAGDIWG-------EIDTRFSFCAVATFALLGKLDA- 161
Cdd:cd00688  80 PSLWLTAYALKALLLagdYIAVDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDPd 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  162 INVEKAIEFVLSCMNFDGGFGcrPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPE---KLPD 238
Cdd:cd00688 160 PLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnKLSD 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1216504  239 VCYSWWVLASLKIIGRL-HWIDREKLRNFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd00688 238 SCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 46-301 5.76e-69

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


Pssm-ID: 239225 [Multi-domain]  Cd Length: 307  Bit Score: 217.53  E-value: 5.76e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   46 RMSGIYWGLTVMDLMGQLHRM---NREEILAFIKSCQ----HECGGISASIGHD----------PHLLYTLSAVQIL-TL 107
Cdd:cd02895  26 RLTIAFFALSGLDLLGALDSIlveEKDDIIEWIYSLQvlsnLPRGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLlIL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  108 YDSINVIDVNKVVEYVKGLQKEDGSFAGDIW---GEIDTRFSFCAVATFALLG--KLDAINVEKAIEFVLSCMNFDGGFG 182
Cdd:cd02895 106 GDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYMLDdwSEEDIDKEKLIDYIKSSQSYDGGFG 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  183 CRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGW---WLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWID 259
Cdd:cd02895 186 QGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERlkrWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLID 265

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 1216504  260 REKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd02895 266 FEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 50-300 1.21e-62

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: 200.92  E-value: 1.21e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   50 IYWGLTVMDLMG-QLHRMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTL---YDSINVIDVNKVVEYVKG 125
Cdd:cd02893  30 LYWILHSLELLGeELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTYAAVNALAIigtEEAYDVIDREALYKFLLS 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  126 LQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITS 205
Cdd:cd02893 110 LKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILG 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  206 QLHQVNSDLLGWWLCERQLPS-GGLNGRPEKLPDVCYSWWVLASLKIIGRL------------HW-IDREKLRNFILACQ 271
Cdd:cd02893 190 KPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPILEAIlnaekkfddsaeGTlFDQEALQEYILLCC 269

                       250       260
                ....*....|....*....|....*....
gi 1216504  272 DEETGGFADRPGDMVDPFHTLFGIAGLSL 300
Cdd:cd02893 270 QSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 21-299 3.10e-31

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 121.82  E-value: 3.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    21 EKHADYIASyGSKKDDYEYCMSEYLRMSGIYWGLTVMDLMGQLHRMNRE-EILAFIKSCQHECGGISASIGHDPHLLYTL 99
Cdd:PLN02710  47 EKHLEYLTR-GLRQLGPSFSVLDANRPWLCYWILHSIALLGESLDDELEnDTIDFLSRCQDPNGGYGGGPGQLPHLATTY 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   100 SAVQIL-TL--YDSINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGKLDAINVEKAIEFVLSCMN 176
Cdd:PLN02710 126 AAVNTLvTIggERALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   177 FDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLH 256
Cdd:PLN02710 206 YEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFALLQQLV 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   257 WIDREK-----------------------------------------------------------LRNFILACQDEETGG 277
Cdd:PLN02710 286 TIVDEQlqtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnqqmgplfhsiaLQQYILLCSQVLDGG 365

                        330       340
                 ....*....|....*....|..
gi 1216504   278 FADRPGDMVDPFHTLFGIAGLS 299
Cdd:PLN02710 366 LRDKPGKSRDYYHTCYCLSGLS 387
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 68-302 9.49e-27

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 105.94  E-value: 9.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   68 REEILAFIKSCQHECGGISASIGhDPHLLYTLSAVQILTLYDSINVIDvNKVVEYVKGLQKEDGSFA-------GDIWGe 140
Cdd:COG5029  21 TDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH- 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  141 idtrfSFCAVATFALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLC 220
Cdd:COG5029  98 -----TYLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLR 171

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  221 ERQLPSGGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRNFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGL 298
Cdd:COG5029 172 DVQSPEGGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGAL 249


                ....
gi 1216504  299 SLLG 302
Cdd:COG5029 250 ALLG 253
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
65-304 4.92e-20

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 87.86  E-value: 4.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   65 RMNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYDsINVIDVNKVVEYVKGLQKEDGSFAGdiwgeidTR 144
Cdd:COG1689   5 RFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLG-EEVPNRDKTIEFLESCQDEEGGGFA-------LY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  145 FSFCAVATFALLGKLDAINVEkAIEFvLSCMNFDGgfgcRPGSESHAGQIYCCT-GFLAitsqLHQVNSDLLGW--WLCE 221
Cdd:COG1689  77 TTSYGLMALALLGIDPPDEQE-ALEY-LSDALPTK----FAGGASDLEETYLAVaLLEA----LGASEPEREKIreFLLS 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  222 RQLPSGGLNGrpeKLPDVCYSWWVLASLKIIGRlHWIDREKLRNFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:COG1689 147 LRRPDGGFGG---KKPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQN-EDGGFSKTPGSYSDLEATYYALRALKLL 221


                ...
gi 1216504  302 GEE 304
Cdd:COG1689 222 GEP 224
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 12-255 8.83e-20

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 87.07  E-value: 8.83e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   12 SDAPDTLLLEKHADYIASygSKKDDyeycmSEYLRMSG------IYWGLTVMDLMGQLHRmNREEILAFIKSCQHECGG- 84
Cdd:COG5029  13 SSKSTADFTDSHLDYLRA--SQNPD-----GGFAGRSGpsdlysTYYAVRTLALLGESPK-WRDRVADLLSSLRVEDGGf 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   85 ------ISASIGHdpHLLYTLSAVqiltLYDsINVIDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLGK 158
Cdd:COG5029  85 akapegGAGSTYH--TYLATLLAE----LLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  159 LDAINVEKAIEFVLSCMNFDGGFGCRPgSESHAGQIYCCTGfLAITSQLHQVNSDL--LGWWLCERQLPSGGLNGRP-EK 235
Cdd:COG5029 158 LDDPIETKVIRFLRDVQSPEGGFAYNT-RIGEADLLSTFTA-ILTLYDLGAAPKLVddLQAYILSLQLPDGGFEGAPwDG 235

                       250       260
                ....*....|....*....|
gi 1216504  236 LPDVCYSWWVLASLKIIGRL 255
Cdd:COG5029 236 VEDVEYTFYGVGALALLGAL 255
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
50-185 3.89e-13

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 68.60  E-value: 3.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   50 IYWGLTVMDLMGQLHRMnREEILAFIKSCQHECGGISASighDPHLLYTLSAVQILTLYDsINVIDVNKVVEYVKGLQKE 129
Cdd:COG1689 120 TYLAVALLEALGASEPE-REKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRLG-RDLPPADRVIAFILACQNE 194

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 1216504  130 DGSFA---GDIWgeiDTRFSFCAVATFALLGKlDAINVEKAIEFVLSCMNFDGGFGCRP 185
Cdd:COG1689 195 DGGFSktpGSYS---DLEATYYALRALKLLGE-PPKNVDKLLEFIASCQNSDGGFRRSP 249
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
162-203 1.83e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.99  E-value: 1.83e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1216504    162 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 203
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
258-302 2.49e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.91  E-value: 2.49e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1216504    258 IDREKLRNFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLG 302
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
210-253 4.21e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.14  E-value: 4.21e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1216504    210 VNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
114-157 5.45e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 56.75  E-value: 5.45e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1216504    114 IDVNKVVEYVKGLQKEDGSFAGDIWGEIDTRFSFCAVATFALLG 157
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 158-303 1.65e-10

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 60.49  E-value: 1.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  158 KLDAINVEKAIEFVLSCMNFDGGFGCRPGsESHAGQIYCCTGFLAITSQLHQVNSDLLGWWL-CERqlPSGGLNGRPEKL 236
Cdd:COG5029  15 KSTADFTDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRV--EDGGFAKAPEGG 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1216504  237 PDVCY-SWWVLASLKIIGRlHWIDREKLRNFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLGE 303
Cdd:COG5029  92 AGSTYhTYLATLLAELLGR-PPPDPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGALRALGA 157
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
66-109 1.71e-09

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 52.51  E-value: 1.71e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1216504     66 MNREEILAFIKSCQHECGGISASIGHDPHLLYTLSAVQILTLYD 109
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 220-310 3.34e-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: 51.04  E-value: 3.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  220 CERQLPSGGLNGRPEKLpdvCYSWWVLASLKIIGR-LHWIDREKLRNFILACQDEETGGFADRPGDMVDPFHTLFGIAGL 298
Cdd:cd02890  11 CLKLLPSSYTSLDASRL---WLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSL 87

                        90
                ....*....|..
gi 1216504  299 SLLGEEQIKPVN 310
Cdd:cd02890  88 AILGDDALSRID 99
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 150-303 1.99e-06

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 49.01  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   150 VATFALLGKLDAINVEK-AIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFL-AITSQ--LHQVNSDLLGWWLCERQLP 225
Cdd:PLN02710  79 LHSIALLGESLDDELENdTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLvTIGGEraLSSINREKLYTFLLRMKDP 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   226 SGGLNGRPEKLPDV--CYSWWVLASLkiigrLHWIDRE---KLRNFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSL 300
Cdd:PLN02710 159 SGGFRMHDGGEMDVraCYTAISVASL-----LNILDDElvkGVGDYILSCQTYE-GGIGGEPGAEAHGGYTFCGLAAMIL 232


                 ...
gi 1216504   301 LGE 303
Cdd:PLN02710 233 INE 235
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 3.43e-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: 45.51  E-value: 3.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504     98 TLSAVQILTLY----DSI-NVIdvNKVVEYVKGLQKEDGSFAGDiWGEIDTRFSFCAVATFALLGKL--DAINVEKAIEF 170
Cdd:TIGR01787 441 TARVIQALGAFghraDEIrNVL--ERALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDW 517

                          90
                  ....*....|..
gi 1216504    171 VLSCMNFDGGFG 182
Cdd:TIGR01787 518 LLSRQMPDGGWG 529
PLN03012 PLN03012
Camelliol C synthase
 98-182 4.11e-05

Camelliol C synthase


Pssm-ID: 166653 [Multi-domain]  Cd Length: 759  Bit Score: 45.39  E-value: 4.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    98 TLSAVQILTLY---------DSINVIdVNKVVEYVKGLQKEDGSFAGDiWGEIDTRFSFCAVATFALLGKL--DAINVEK 166
Cdd:PLN03012 566 TSSAIQALILFkqlypdhrtEEINAF-IKKAAEYIENIQMLDGSWYGN-WGICFTYGTWFALAGLAAAGKTfnDCEAIRK 643

                         90
                 ....*....|....*.
gi 1216504   167 AIEFVLSCMNFDGGFG 182
Cdd:PLN03012 644 GVHFLLAAQKDNGGWG 659
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 51-160 1.46e-04

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 42.77  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   51 YWGLTVMDLMGQLHRMNREEILAFIKSCQHECGGISA--SIGhDPHLLYTLSAvqILTLYD-SINVIDVNKVVEYVKGLQ 127
Cdd:COG5029 146 AAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYntRIG-EADLLSTFTA--ILTLYDlGAAPKLVDDLQAYILSLQ 222

                        90       100       110
                ....*....|....*....|....*....|....
gi 1216504  128 KEDGSFAGDIWGEI-DTRFSFCAVATFALLGKLD 160
Cdd:COG5029 223 LPDGGFEGAPWDGVeDVEYTFYGVGALALLGALA 256
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 116-227 4.06e-04

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: 41.82  E-value: 4.06e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  116 VNKVVEYVKGLQKEDGSFAGDiWGeID----TRFSFCAVATFALLGKLDAINveKAIEFVLSCMNFDGGFG--CrpgsES 189
Cdd:cd02889 193 IRRAVKYLEREQEPDGSWYGR-WG-VCfiygTWFALEALAAAGEDENSPYVR--KACDWLLSKQNPDGGWGesY----ES 264

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 1216504  190 HAGQIYCCTGflaiTSQLHQVnsdllGW---------------------WLCERQLPSG 227
Cdd:cd02889 265 YEDPSYAGGG----RSTVVQT-----AWallalmaagepdseavkrgvkYLLNTQQEDG 314
SQCY_1 cd02892
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
 116-227 8.44e-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: 41.03  E-value: 8.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504  116 VNKVVEYVKGLQKEDGSFAGDiWGeidTRFSFcavATFALLGKLDAIN--------VEKAIEFVLSCMNFDGGFG----- 182
Cdd:cd02892 478 IRRAVKYLLREQEPDGSWYGR-WG---VCYIY---GTWFALEALAAAGedyenspyIRKACDFLLSKQNPDGGWGesyls 550

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 1216504  183 CRPGS--ESHAGQIyCCTGFlAITSQLH--QVNSDLL--GW-WLCERQLPSG 227
Cdd:cd02892 551 YEDKSyaGGGRSTV-VQTAW-ALLALMAagEPDSEAVerGIkYLLNTQLPDG 600
osq_cycl TIGR03463
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ...
 116-228 2.89e-03

2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella aurantiaca which produces cycloartenol, and Gemmata obscuriglobus and Methylococcus capsulatus, which each produce the closely related sterol, lanosterol.


Pssm-ID: 274591 [Multi-domain]  Cd Length: 634  Bit Score: 39.21  E-value: 2.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504    116 VNKVVEYVKGLQKEDGSFAGdIWGEIDTRFSFCAVATFALLG-KLDAINVEKAIEFVLSCMNFDGGFG-----CRPGS-- 187
Cdd:TIGR03463 479 IRKAEEFIRRRQLDDGSFMG-FWGICFTYATFFGAKGLIAAGaEPADMALQAAAAFLLEKQRADGAWGehvesCLEARwv 557

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1216504    188 ESHAGQIYCCTGFLAITSQLHQVNSDLLG---WWLCERQLPSGG 228
Cdd:TIGR03463 558 EGKHGHAVMTAWALLALAAAGEAAHDAAErgiAWLCEQQGEDGG 601
hopene_cyclase TIGR01507
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ...
 116-182 4.37e-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: 38.72  E-value: 4.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216504    116 VNKVVEYVKGLQKEDGSFAGDiWGeidTRFSFCAVATFALLGKLDAIN----VEKAIEFVLSCMNFDGGFG 182
Cdd:TIGR01507 473 IERAVEYLKREQEPDGSWFGR-WG---VNYLYGTGAVLSALKAVGIDTrepyIQKALAWLESHQNPDGGWG 539
A2M_like cd02891
Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier ...
 57-176 6.00e-03

Proteins similar to alpha2-macroglobulin (alpha (2)-M). Alpha (2)-M is a major carrier protein in serum. It is a broadly specific proteinase inhibitor. The structural thioester of alpha (2)-M, is involved in the immobilization and entrapment of proteases. This group contains another broadly specific proteinase inhibitor: pregnancy zone protein (PZP). PZP is a trace protein in the plasma of non-pregnant females and males which is elevated in pregnancy. Alpha (2)-M and PZ bind to placental protein-14 and may modulate its activity in T-cell growth and cytokine production thereby protecting the allogeneic fetus from attack by the maternal immune system. This group also contains C3, C4 and C5 of vertebrate complement. The vertebrate complement is an effector of both the acquired and innate immune systems The point of convergence of the classical, alternative and lectin pathways of the complement system is the proteolytic activation of C3. C4 plays a key role in propagating the classical and lectin pathways. C5 participates in the classical and alternative pathways. The thioester bond located within the structure of C3 and C4 is central to the function of complement. C5 does not contain an active thioester bond.


Pssm-ID: 239221 [Multi-domain]  Cd Length: 282  Bit Score: 37.75  E-value: 6.00e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1216504   57 MDLMGQLHRMNREEILAFIK-------SCQHECGGISASIGHDPHLLYtLSA--VQILTL---YDSINVIDVNKVVEYVK 124
Cdd:cd02891  33 LDATGQLTPEIREKALEYIRkgyqrllTYQRSDGSFSAWGNSDSGSTW-LTAyvVKFLSQarkYIDVDENVLARALGWLV 111

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1216504  125 GLQKEDGSF-------AGDIWGEIDTRFSFCAVATFALL--GKLDAINVEKAIEFVLSCMN 176
Cdd:cd02891 112 PQQKEDGSFrelgpviHREMKGGVDDSVSLTAYVLIALAeaGKACDASIEKALAYLETQLD 172
PLN02993 PLN02993
lupeol synthase
 116-190 7.00e-03

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 38.35  E-value: 7.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1216504   116 VNKVVEYVKGLQKEDGSFAGDiWGEIDTRFSFCAVATFALLGKL--DAINVEKAIEFVLSCMNFDGGFGcrpgsESH 190
Cdd:PLN02993 592 IEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAGKTynDCLAMRKGVHFLLTIQRDDGGWG-----ESY 662
 
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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