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Conserved domains on  [gi|730317|sp|Q08603|]
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RecName: Full=Geranylgeranyl transferase type-2 subunit beta; AltName: Full=Geranylgeranyl transferase type II subunit beta; Short=GGTase-II-beta; AltName: Full=Rab geranyl-geranyltransferase subunit beta; Short=Rab GG transferase beta; Short=Rab GGTase beta; AltName: Full=Rab geranylgeranyltransferase subunit beta; AltName: Full=Type II protein geranyl-geranyltransferase subunit beta

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: 545.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    18 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKEEILVFIKSCQ-HECGGVSASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    97 YTLSAVQILTLYDSIHVI--NVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   175 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 730317   255 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 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: 545.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    18 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKEEILVFIKSCQ-HECGGVSASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    97 YTLSAVQILTLYDSIHVI--NVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   175 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 730317   255 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 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: 512.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     14 APDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKEEILVFIKSCQHECGGVSASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     94 HLLYTLSAVQILTLYDSIHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    174 CMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    254 RLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRV 323
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 74-302 5.02e-28

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 109.41  E-value: 5.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    74 FIKSCQHECGGVSASIGhDPHLLYTLSAVQILTLYDSIHVINvDKVVAYVQSLQKEDGSFA-------GDIWGeidtrfS 146
Cdd:COG5029  27 YLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH------T 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   147 FCAVATLALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPS 226
Cdd:COG5029  99 YLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPE 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730317   227 GGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGLSLLG 302
Cdd:COG5029 178 GGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
162-203 2.04e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.99  E-value: 2.04e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 730317     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 2.40e-04

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: 42.81  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317      98 TLSAVQILTLY----DSI-HVINvdKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKAIEF 170
Cdd:TIGR01787 441 TARVIQALGAFghraDEIrNVLE--RALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDW 517

                          90
                  ....*....|..
gi 730317     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: 545.71  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    18 LLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKEEILVFIKSCQ-HECGGVSASIGHDPHLL 96
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQdNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    97 YTLSAVQILTLYDSIHVI--NVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSC 174
Cdd:cd02894  81 STLSAIQILALYDLLNKIdeNKEKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   175 MNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLKIIGR 240

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 730317   255 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 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: 512.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     14 APDTLLLEKHADYIASYGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKEEILVFIKSCQHECGGVSASIGHDP 93
Cdd:PLN03201   4 PMGELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHESGGFGGNTGHDP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     94 HLLYTLSAVQILTLYDSIHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLS 173
Cdd:PLN03201  84 HILYTLSAVQILALFDRLDLLDADKVASYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIVS 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    174 CMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:PLN03201 164 CKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLLGWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSLIIID 243

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    254 RLHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLLGEEQIKPVSPVFCMPEEVLQRV 323
Cdd:PLN03201 244 RVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDVVNRI 313
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 20-301 6.26e-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: 6.26e-149
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    20 LEKHADYIASYGsKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQ-LHRMNKEEILVFIKSCQ-HECGGVSASIGHDPHLLY 97
Cdd:cd02890   1 REKHIKYLQRCL-KLLPSSYTSLDASRLWLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQvNEDGGFGGGPGQDPHLAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    98 TLSAVQILTLYDS--IHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCM 175
Cdd:cd02890  80 TYAAVLSLAILGDdaLSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSCQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   176 NFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSG-GLNGRPEKLPDVCYSWWVLASLKIIGR 254
Cdd:cd02890 160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGgGFNGRPNKLVDTCYSFWVGASLKILGR 239

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 730317   255 LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd02890 240 LHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 20-301 1.42e-77

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: 239.37  E-value: 1.42e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    20 LEKHADYIASYGsKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLH------RMNKEEILVFIKSCQHECGGVSASIGHD- 92
Cdd:cd00688   1 IEKHLKYLLRYP-YGDGHWYQSLCGEQTWSTAWPLLALLLLLAATgirdkaDENIEKGIQRLLSYQLSDGGFSGWGGNDy 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    93 PHLLYTLSAVQILTL---YDSIHVINVDKVVAYVQSLQKEDGSFAGDIWG-------EIDTRFSFCAVATLALLGKLDA- 161
Cdd:cd00688  80 PSLWLTAYALKALLLagdYIAVDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDPd 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   162 INVEKAIEFVLSCMNFDGGFGcrPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPE---KLPD 238
Cdd:cd00688 160 PLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRDrtnKLSD 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 730317   239 VCYSWWVLASLKIIGRL-HWIDREKLRSFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd00688 238 SCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQN-EDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 46-301 1.81e-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: 219.07  E-value: 1.81e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    46 RMSGVYWGLTVMDLMGQLHRM---NKEEILVFIKSCQ----HECGGVSASIGHD----------PHLLYTLSAVQIL-TL 107
Cdd:cd02895  26 RLTIAFFALSGLDLLGALDSIlveEKDDIIEWIYSLQvlsnLPRGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLlIL 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   108 YDSIHVINVDKVVAYVQSLQKEDGSFAGDIW---GEIDTRFSFCAVATLALLG--KLDAINVEKAIEFVLSCMNFDGGFG 182
Cdd:cd02895 106 GDDLSRVDRKAILNFLSKLQLPDGSFGSVLDsegGENDMRFCYCAVAICYMLDdwSEEDIDKEKLIDYIKSSQSYDGGFG 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   183 CRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGW---WLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLHWID 259
Cdd:cd02895 186 QGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERlkrWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLID 265

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 730317   260 REKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:cd02895 266 FEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 50-300 3.02e-63

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: 202.47  E-value: 3.02e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    50 VYWGLTVMDLMG-QLHRMNKEEILVFIKSCQHECGGVSASIGHDPHLLYTLSAVQILTL---YDSIHVINVDKVVAYVQS 125
Cdd:cd02893  30 LYWILHSLELLGeELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTYAAVNALAIigtEEAYDVIDREALYKFLLS 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   126 LQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITS 205
Cdd:cd02893 110 LKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELFEGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILG 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   206 QLHQVNSDLLGWWLCERQLPS-GGLNGRPEKLPDVCYSWWVLASLKIIGRL------------HW-IDREKLRSFILACQ 271
Cdd:cd02893 190 KPDKLDLESLLRWLVARQMRFeGGFQGRTNKLVDGCYSFWVGGSLPILEAIlnaekkfddsaeGTlFDQEALQEYILLCC 269

                       250       260
                ....*....|....*....|....*....
gi 730317   272 DEETGGFADRPGDMVDPFHTLFGIAGLSL 300
Cdd:cd02893 270 QSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 21-299 1.43e-30

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 119.89  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     21 EKHADYIASyGSKKDDYEYCMSEYLRMSGVYWGLTVMDLMGQLHRMNKE-EILVFIKSCQHECGGVSASIGHDPHLLYTL 99
Cdd:PLN02710  47 EKHLEYLTR-GLRQLGPSFSVLDANRPWLCYWILHSIALLGESLDDELEnDTIDFLSRCQDPNGGYGGGPGQLPHLATTY 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    100 SAVQIL-TL--YDSIHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGKLDAINVEKAIEFVLSCMN 176
Cdd:PLN02710 126 AAVNTLvTIggERALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNILDDELVKGVGDYILSCQT 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    177 FDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIGRLH 256
Cdd:PLN02710 206 YEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSLINWVVFRQGVEGGFQGRTNKLVDGCYSFWQGGVFALLQQLV 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    257 WIDREK-----------------------------------------------------------LRSFILACQDEETGG 277
Cdd:PLN02710 286 TIVDEQlqtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnqqmgplfhsiaLQQYILLCSQVLDGG 365

                        330       340
                 ....*....|....*....|..
gi 730317    278 FADRPGDMVDPFHTLFGIAGLS 299
Cdd:PLN02710 366 LRDKPGKSRDYYHTCYCLSGLS 387
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 74-302 5.02e-28

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 109.41  E-value: 5.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    74 FIKSCQHECGGVSASIGhDPHLLYTLSAVQILTLYDSIHVINvDKVVAYVQSLQKEDGSFA-------GDIWGeidtrfS 146
Cdd:COG5029  27 YLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR-DRVADLLSSLRVEDGGFAkapeggaGSTYH------T 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   147 FCAVATLALLGKLDAInVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAITSQLHQVNSDLLGWWLCERQLPS 226
Cdd:COG5029  99 YLATLLAELLGRPPPD-PDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPE 177

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730317   227 GGLNGRPEK-LPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMV-DPFHTLFGIAGLSLLG 302
Cdd:COG5029 178 GGFAYNTRIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPD-GGFEGAPWDGVeDVEYTFYGVGALALLG 253
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
65-304 3.57e-21

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 91.32  E-value: 3.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    65 RMNKEEILVFIKSCQHECGGVSASIGHDPHLLYTLSAVQILTLYDsIHVINVDKVVAYVQSLQKEDGSFAGdiwgeidTR 144
Cdd:COG1689   5 RFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLG-EEVPNRDKTIEFLESCQDEEGGGFA-------LY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   145 FSFCAVATLALLGKLDAINVEkAIEFvLSCMNFDGgfgcRPGSESHAGQIYCCT-GFLAitsqLHQVNSDLLGW--WLCE 221
Cdd:COG1689  77 TTSYGLMALALLGIDPPDEQE-ALEY-LSDALPTK----FAGGASDLEETYLAVaLLEA----LGASEPEREKIreFLLS 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   222 RQLPSGGLNGrpeKLPDVCYSWWVLASLKIIGRlHWIDREKLRSFILACQDeETGGFADRPGDMVDPFHTLFGIAGLSLL 301
Cdd:COG1689 147 LRRPDGGFGG---KKPNLEDTYWALAALRRLGR-DLPPADRVIAFILACQN-EDGGFSKTPGSYSDLEATYYALRALKLL 221


                ...
gi 730317   302 GEE 304
Cdd:COG1689 222 GEP 224
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 12-255 1.78e-19

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 86.30  E-value: 1.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    12 SDAPDTLLLEKHADYIASygSKKDDyeycmSEYLRMSG------VYWGLTVMDLMGQLHRmNKEEILVFIKSCQHECGG- 84
Cdd:COG5029  13 SSKSTADFTDSHLDYLRA--SQNPD-----GGFAGRSGpsdlysTYYAVRTLALLGESPK-WRDRVADLLSSLRVEDGGf 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    85 ------VSASIGHdpHLLYTLSAVqiltLYDsIHVINVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLGK 158
Cdd:COG5029  85 akapegGAGSTYH--TYLATLLAE----LLG-RPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   159 LDAINVEKAIEFVLSCMNFDGGFGCRPgSESHAGQIYCCTGfLAITSQLHQVNSDL--LGWWLCERQLPSGGLNGRP-EK 235
Cdd:COG5029 158 LDDPIETKVIRFLRDVQSPEGGFAYNT-RIGEADLLSTFTA-ILTLYDLGAAPKLVddLQAYILSLQLPDGGFEGAPwDG 235

                       250       260
                ....*....|....*....|
gi 730317   236 LPDVCYSWWVLASLKIIGRL 255
Cdd:COG5029 236 VEDVEYTFYGVGALALLGAL 255
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
50-185 2.05e-13

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 69.37  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    50 VYWGLTVMDLMGQLHRMnKEEILVFIKSCQHECGGVSASighDPHLLYTLSAVQILTLYDsIHVINVDKVVAYVQSLQKE 129
Cdd:COG1689 120 TYLAVALLEALGASEPE-REKIREFLLSLRRPDGGFGGK---KPNLEDTYWALAALRRLG-RDLPPADRVIAFILACQNE 194

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 730317   130 DGSFA---GDIWgeiDTRFSFCAVATLALLGKlDAINVEKAIEFVLSCMNFDGGFGCRP 185
Cdd:COG1689 195 DGGFSktpGSYS---DLEATYYALRALKLLGE-PPKNVDKLLEFIASCQNSDGGFRRSP 249
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
162-203 2.04e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 60.99  E-value: 2.04e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 730317     162 INVEKAIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFLAI 203
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALAL 42
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
114-157 3.89e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.14  E-value: 3.89e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 730317     114 INVDKVVAYVQSLQKEDGSFAGDIWGEIDTRFSFCAVATLALLG 157
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
210-253 4.74e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 57.14  E-value: 4.74e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 730317     210 VNSDLLGWWLCERQLPSGGLNGRPEKLPDVCYSWWVLASLKIIG 253
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
258-302 7.93e-11

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 56.37  E-value: 7.93e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 730317     258 IDREKLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLG 302
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 158-303 1.44e-10

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 60.88  E-value: 1.44e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   158 KLDAINVEKAIEFVLSCMNFDGGFGCRPGsESHAGQIYCCTGFLAITSQLHQVNSDLLGWWL-CERqlPSGGLNGRPEKL 236
Cdd:COG5029  15 KSTADFTDSHLDYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWRDRVADLLSsLRV--EDGGFAKAPEGG 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 730317   237 PDVCY-SWWVLASLKIIGRlHWIDREKLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSLLGE 303
Cdd:COG5029  92 AGSTYhTYLATLLAELLGR-PPPDPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGALRALGA 157
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
66-109 7.31e-08

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 47.89  E-value: 7.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 730317      66 MNKEEILVFIKSCQHECGGVSASIGHDPHLLYTLSAVQILTLYD 109
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 220-309 1.10e-06

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: 49.50  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   220 CERQLPSGGLNGRPEKLpdvCYSWWVLASLKIIGR-LHWIDREKLRSFILACQDEETGGFADRPGDMVDPFHTLFGIAGL 298
Cdd:cd02890  11 CLKLLPSSYTSLDASRL---WLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSL 87

                        90
                ....*....|.
gi 730317   299 SLLGEEQIKPV 309
Cdd:cd02890  88 AILGDDALSRI 98
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 150-303 3.62e-06

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 48.24  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    150 VATLALLGKLDAINVEK-AIEFVLSCMNFDGGFGCRPGSESHAGQIYCCTGFL-AITSQ--LHQVNSDLLGWWLCERQLP 225
Cdd:PLN02710  79 LHSIALLGESLDDELENdTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLvTIGGEraLSSINREKLYTFLLRMKDP 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    226 SGGLNGRPEKLPDV--CYSWWVLASLkiigrLHWIDRE---KLRSFILACQDEEtGGFADRPGDMVDPFHTLFGIAGLSL 300
Cdd:PLN02710 159 SGGFRMHDGGEMDVraCYTAISVASL-----LNILDDElvkGVGDYILSCQTYE-GGIGGEPGAEAHGGYTFCGLAAMIL 232


                 ...
gi 730317    301 LGE 303
Cdd:PLN02710 233 INE 235
PLN03012 PLN03012
Camelliol C synthase
 98-182 6.76e-06

Camelliol C synthase


Pssm-ID: 166653 [Multi-domain]  Cd Length: 759  Bit Score: 47.70  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     98 TLSAVQILTLYDSIH--------VINVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKA 167
Cdd:PLN03012 566 TSSAIQALILFKQLYpdhrteeiNAFIKKAAEYIENIQMLDGSWYGN-WGICFTYGTWFALAGLAAAGKTfnDCEAIRKG 644

                         90
                 ....*....|....*
gi 730317    168 IEFVLSCMNFDGGFG 182
Cdd:PLN03012 645 VHFLLAAQKDNGGWG 659
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 51-160 3.08e-05

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 44.70  E-value: 3.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    51 YWGLTVMDLMGQLHRMNKEEILVFIKSCQHECGGVSA--SIGhDPHLLYTLSAVQILtlyDSIHV--INVDKVVAYVQSL 126
Cdd:COG5029 146 AAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYntRIG-EADLLSTFTAILTL---YDLGAapKLVDDLQAYILSL 221

                        90       100       110
                ....*....|....*....|....*....|....*
gi 730317   127 QKEDGSFAGDIWGEI-DTRFSFCAVATLALLGKLD 160
Cdd:COG5029 222 QLPDGGFEGAPWDGVeDVEYTFYGVGALALLGALA 256
PLN02993 PLN02993
lupeol synthase
 98-190 1.18e-04

lupeol synthase


Pssm-ID: 215537 [Multi-domain]  Cd Length: 763  Bit Score: 43.75  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     98 TLSAVQILTLYDSIH--------VINVDKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKA 167
Cdd:PLN02993 566 TSAVIQALVLFKQLYpdhrtkeiIKSIEKAVQFIESKQTPDGSWYGN-WGICFIYATWFALGGLAAAGKTynDCLAMRKG 644

                         90       100
                 ....*....|....*....|...
gi 730317    168 IEFVLSCMNFDGGFGcrpgsESH 190
Cdd:PLN02993 645 VHFLLTIQRDDGGWG-----ESY 662
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 98-182 2.40e-04

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: 42.81  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317      98 TLSAVQILTLY----DSI-HVINvdKVVAYVQSLQKEDGSFAGDiWGEIDTRFSFCAVATLALLGKL--DAINVEKAIEF 170
Cdd:TIGR01787 441 TARVIQALGAFghraDEIrNVLE--RALEYLRREQRADGSWFGR-WGVNYTYGTGFVLSALAAAGRTyrNCPEVQKACDW 517

                          90
                  ....*....|..
gi 730317     171 VLSCMNFDGGFG 182
Cdd:TIGR01787 518 LLSRQMPDGGWG 529
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 98-227 1.08e-03

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: 40.28  E-value: 1.08e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317    98 TLSAVQILTL---YDSIHVINVDKVVA----YVQSLQKEDGSFAGDiWGeID----TRFSFCAvatLALLGKLDAIN-VE 165
Cdd:cd02889 168 TGSVLEALGLfgkLYPEHRREIDPAIRravkYLEREQEPDGSWYGR-WG-VCfiygTWFALEA---LAAAGEDENSPyVR 242

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317   166 KAIEFVLSCMNFDGGFG--CrpgsESHAGQIYCCTGflaiTSQLHQVnsdllGW---------------------WLCER 222
Cdd:cd02889 243 KACDWLLSKQNPDGGWGesY----ESYEDPSYAGGG----RSTVVQT-----AWallalmaagepdseavkrgvkYLLNT 309


                ....*
gi 730317   223 QLPSG 227
Cdd:cd02889 310 QQEDG 314
osq_cycl TIGR03463
2,3-oxidosqualene cyclase; This model identifies 2,3-oxidosqualene cyclases from Stigmatella ...
 116-228 2.00e-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: 39.98  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 730317     116 VDKVVAYVQSLQKEDGSFAGdIWGEIDTRFSFCAVATLALLG-KLDAINVEKAIEFVLSCMNFDGGFG-----CRPGS-- 187
Cdd:TIGR03463 479 IRKAEEFIRRRQLDDGSFMG-FWGICFTYATFFGAKGLIAAGaEPADMALQAAAAFLLEKQRADGAWGehvesCLEARwv 557

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 730317     188 ESHAGQIYCCTGFLAITSQLHQVNSDLLG---WWLCERQLPSGG 228
Cdd:TIGR03463 558 EGKHGHAVMTAWALLALAAAGEAAHDAAErgiAWLCEQQGEDGG 601
 
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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