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Conserved domains on  [gi|6325434|ref|NP_015502|]
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Rab geranylgeranyltransferase BET2 [Saccharomyces cerevisiae S288C]

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 ...
 7-297 7.70e-178

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: 493.32  E-value: 7.70e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    7 LLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKYGAFAPFPRHDAHLL 86
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQDNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   87 TTLSAVQILATYDALDVLGKDRkVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLK 166
Cdd:cd02894  81 STLSAIQILALYDLLNKIDENK-EKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  167 CYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLeeiGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLA 246
Cdd:cd02894 160 CYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRL---GWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLK 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6325434  247 IIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLM 297
Cdd:cd02894 237 IIGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 7-297 7.70e-178

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: 493.32  E-value: 7.70e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    7 LLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKYGAFAPFPRHDAHLL 86
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQDNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   87 TTLSAVQILATYDALDVLGKDRkVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLK 166
Cdd:cd02894  81 STLSAIQILALYDLLNKIDENK-EKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  167 CYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLeeiGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLA 246
Cdd:cd02894 160 CYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRL---GWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLK 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6325434  247 IIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLM 297
Cdd:cd02894 237 IIGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 6-315 3.65e-155

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 436.82  E-value: 3.65e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434     6 TLLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKyGAFAPFPRHDAHL 85
Cdd:PLN03201   7 ELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHES-GGFGGNTGHDPHI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    86 LTTLSAVQILATYDALDVLGKDRKVrliSFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVL 165
Cdd:PLN03201  86 LYTLSAVQILALFDRLDLLDADKVA---SYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   166 KCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLeeiGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSL 245
Cdd:PLN03201 163 SCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLL---GWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSL 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   246 AIIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLMGYDNLVPIDPIYCMPKSV 315
Cdd:PLN03201 240 IIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDV 309
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 73-298 2.01e-22

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 94.39  E-value: 2.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   73 GAFAPFPRhDAHLLTTLSAVQILAtydaldVLGKDRKV--RLISFIRGNQLEDGSF-QGDRFGEVDTRFVYTALSALSIL 149
Cdd:COG5029  36 GGFAGRSG-PSDLYSTYYAVRTLA------LLGESPKWrdRVADLLSSLRVEDGGFaKAPEGGAGSTYHTYLATLLAELL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  150 GElTSEVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDmlsDDQLEEIGWWLCERQLPEGGLNGRP 229
Cdd:COG5029 109 GR-PPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD---DPIETKVIRFLRDVQSPEGGFAYNT 184

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325434  230 SK-LPDVCYSWWVLSSLAIIGRlDWINYEKLTEFILKCQ-DEkkGGISDRPENEV-DVFHTVFGVAGLSLMG 298
Cdd:COG5029 185 RIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQlPD--GGFEGAPWDGVeDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
209-249 4.42e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 59.83  E-value: 4.42e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6325434    209 EEIGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLAIIG 249
Cdd:pfam00432   4 EKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 111-226 2.26e-03

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: 39.73  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    111 RLISFIRGNQLEDGSFQGdRFGevdTRFVY---TALSALSILGELTSE--VVDPAVDFVLKCYNFDGGFG----LCPN-- 179
Cdd:TIGR01787 464 RALEYLRREQRADGSWFG-RWG---VNYTYgtgFVLSALAAAGRTYRNcpEVQKACDWLLSRQMPDGGWGedcfSYEDps 539

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 6325434    180 -AESHAAQAF-TCLGALAIANKLDMLSDDQLEEIGwWLCERQLPEGGLN 226
Cdd:TIGR01787 540 yVGSGGSTPSqTGWALMALIAAGEADSEAIERGVK-YLLETQRPDGDWP 587
 
Name Accession Description Interval E-value
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 7-297 7.70e-178

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: 493.32  E-value: 7.70e-178
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    7 LLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKYGAFAPFPRHDAHLL 86
Cdd:cd02894   1 LLLEKHIEYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLLGQLERLNREEIIEFVKSCQDNEDGGFGGSPGHDPHIL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   87 TTLSAVQILATYDALDVLGKDRkVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLK 166
Cdd:cd02894  81 STLSAIQILALYDLLNKIDENK-EKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVDKAVDYLLS 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  167 CYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLeeiGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLA 246
Cdd:cd02894 160 CYNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRL---GWWLCERQLPSGGLNGRPEKLPDVCYSWWVLSSLK 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6325434  247 IIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLM 297
Cdd:cd02894 237 IIGRLHWINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLSLL 287
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 6-315 3.65e-155

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 436.82  E-value: 3.65e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434     6 TLLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVLDSPETFVKEEVISFVLSCWDDKyGAFAPFPRHDAHL 85
Cdd:PLN03201   7 ELVVDKHVRYIKSLEKKKDSFESVVMEHLRMNGAYWGLTALDLLGKLDDVDRDEVVSWVMRCQHES-GGFGGNTGHDPHI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    86 LTTLSAVQILATYDALDVLGKDRKVrliSFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVL 165
Cdd:PLN03201  86 LYTLSAVQILALFDRLDLLDADKVA---SYVAGLQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAVDYIV 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   166 KCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLeeiGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSL 245
Cdd:PLN03201 163 SCKNFDGGFGCTPGGESHAGQIFCCVGALAITGSLHHVDKDLL---GWWLCERQVKSGGLNGRPEKLPDVCYSWWVLSSL 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   246 AIIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLMGYDNLVPIDPIYCMPKSV 315
Cdd:PLN03201 240 IIIDRVHWIDKDKLAKFILDCQDDENGGISDRPDDAVDVFHTFFGVAGLSLLGYPGLKPIDPAYALPVDV 309
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 9-297 1.07e-134

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: 383.86  E-value: 1.07e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    9 KEKHIRYIESLDTKKhNFEYWLTEHLRLNGIYWGLTALCVLDSPETF-VKEEVISFVLSCWDDKYGAFAPFPRHDAHLLT 87
Cdd:cd02890   1 REKHIKYLQRCLKLL-PSSYTSLDASRLWLLYWILSSLDLLGEDLDDeNKDEIIDFIYSCQVNEDGGFGGGPGQDPHLAS 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   88 TLSAVQILATYDALDVLGKDRKvRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLKC 167
Cdd:cd02890  80 TYAAVLSLAILGDDALSRIDRE-KIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKEKLIDYILSC 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  168 YNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLsddQLEEIGWWLCERQLP-EGGLNGRPSKLPDVCYSWWVLSSLA 246
Cdd:cd02890 159 QNYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLI---DKERLLRWLVERQLAsGGGFNGRPNKLVDTCYSFWVGASLK 235

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 6325434  247 IIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSLM 297
Cdd:cd02890 236 ILGRLHLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 9-297 2.03e-65

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: 208.17  E-value: 2.03e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    9 KEKHIRYIESLDTKKhNFEYWLTEHLRLNGIYWGLTALCVLDSPETF------VKEEVISFVLSCWDDKyGAFAPFPRHD 82
Cdd:cd00688   1 IEKHLKYLLRYPYGD-GHWYQSLCGEQTWSTAWPLLALLLLLAATGIrdkadeNIEKGIQRLLSYQLSD-GGFSGWGGND 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   83 -AHLLTTLSAVQILATYDALDVLGKDRKVRLISFIRGNQLEDGSFQGDR-------FGEVDTRFVYTALSALSILGELT- 153
Cdd:cd00688  79 yPSLWLTAYALKALLLAGDYIAVDRIDLARALNWLLSLQNEDGGFREDGpgnhrigGDESDVRLTAYALIALALLGKLDp 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  154 SEVVDPAVDFVLKCYNFDGGFGlcPNAESHAAQAFTCLGALAIANKLDMlsdDQLEEIGWWLCERQLPEGGLNGRP---S 230
Cdd:cd00688 159 DPLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDS---PDAKKALRWLLSRQRPDGGWGEGRdrtN 233

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6325434  231 KLPDVCYSWWVLSSLAIIGRL-DWINYEKLTEFILKCQDEkKGGISDRPENEVDVFHTVFGVAGLSLM 297
Cdd:cd00688 234 KLSDSCYTEWAAYALLALGKLgDLEDAEKLVKWLLSQQNE-DGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 9-297 2.41e-63

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: 202.89  E-value: 2.41e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    9 KEKHIRYIE-----------SLDTKkhnfeywltehlRLNGIYWGLTALCVLDSPETFV---KEEVISFVLSC---WDDK 71
Cdd:cd02895   1 KKKHVKFFQrclqllpssyqSLDTN------------RLTIAFFALSGLDLLGALDSILveeKDDIIEWIYSLqvlSNLP 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   72 YGAFAPFPRHD----------AHLLTTLSAVQILAtydaldVLGKD----RKVRLISFIRGNQLEDGSF---QGDRFGEV 134
Cdd:cd02895  69 RGGFRGSSTLGlpgtaskydtGNLAMTYFALLSLL------ILGDDlsrvDRKAILNFLSKLQLPDGSFgsvLDSEGGEN 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  135 DTRFVYTALSALSILGELTSEVVDP--AVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLEEIG 212
Cdd:cd02895 143 DMRFCYCAVAICYMLDDWSEEDIDKekLIDYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEELSEKFLERLK 222

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  213 WWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLAIIGRLDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVA 292
Cdd:cd02895 223 RWLVHRQVSGTGFNGRPNKPADTCYSFWVGASLKLLDAFQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLA 302


                ....*
gi 6325434  293 GLSLM 297
Cdd:cd02895 303 ALSLI 307
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 9-296 3.87e-61

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: 197.07  E-value: 3.87e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    9 KEKHIRYIE-SLDTKKHNFEY------WLtehlrlngIYWGLTALCVLDSP-ETFVKEEVISFVLSCwDDKYGAFAPFPR 80
Cdd:cd02893   1 REKHIKYLKkSLRQLPSSFTSldasrpWL--------LYWILHSLELLGEElDQSYADDVISFLRRC-QNPSGGFGGGPG 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   81 HDAHLLTTLSAVQILA---TYDALDVLgkDRKvRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVV 157
Cdd:cd02893  72 QLPHLATTYAAVNALAiigTEEAYDVI--DRE-ALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTDELF 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  158 DPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLEEigwWLCERQLP-EGGLNGRPSKLPDVC 236
Cdd:cd02893 149 EGVAEYILSCQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLR---WLVARQMRfEGGFQGRTNKLVDGC 225

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6325434  237 YSWWVLSSLAIIGRL------------DW-INYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLSL 296
Cdd:cd02893 226 YSFWVGGSLPILEAIlnaekkfddsaeGTlFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHTCYALSGLSI 298
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 5-309 4.77e-32

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 123.74  E-value: 4.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434     5 LTLLKEKHIRYI-----------ESLDTKKHnfeyWLTehlrlngiYWGLTALCVLDSP-ETFVKEEVISFVLSCwDDKY 72
Cdd:PLN02710  42 LELWREKHLEYLtrglrqlgpsfSVLDANRP----WLC--------YWILHSIALLGESlDDELENDTIDFLSRC-QDPN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    73 GAFAPFPRHDAHLLTTLSAVQILATYDALDVLGKDRKVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGEL 152
Cdd:PLN02710 109 GGYGGGPGQLPHLATTYAAVNTLVTIGGERALSSINREKLYTFLLRMKDPSGGFRMHDGGEMDVRACYTAISVASLLNIL 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   153 TSEVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDMLSDDQLeeIGwWLCERQLPEGGLNGRPSKL 232
Cdd:PLN02710 189 DDELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLPSL--IN-WVVFRQGVEGGFQGRTNKL 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   233 PDVCYSWWVLSSLAIIGRLDWINYEK------------------------------------------------------ 258
Cdd:PLN02710 266 VDGCYSFWQGGVFALLQQLVTIVDEQlqtggssimfeeleddacetsssgkddagdtdsadyskvgfdfikasnqqmgpl 345

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325434   259 -----LTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGLS-------------------LMGYDNLV-PIDPIY 309
Cdd:PLN02710 346 fhsiaLQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLSvaqysaskdedspplprhvLGPYSNLLePIHPLY 421
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 73-298 2.01e-22

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 94.39  E-value: 2.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   73 GAFAPFPRhDAHLLTTLSAVQILAtydaldVLGKDRKV--RLISFIRGNQLEDGSF-QGDRFGEVDTRFVYTALSALSIL 149
Cdd:COG5029  36 GGFAGRSG-PSDLYSTYYAVRTLA------LLGESPKWrdRVADLLSSLRVEDGGFaKAPEGGAGSTYHTYLATLLAELL 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  150 GElTSEVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIANKLDmlsDDQLEEIGWWLCERQLPEGGLNGRP 229
Cdd:COG5029 109 GR-PPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD---DPIETKVIRFLRDVQSPEGGFAYNT 184

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6325434  230 SK-LPDVCYSWWVLSSLAIIGRlDWINYEKLTEFILKCQ-DEkkGGISDRPENEV-DVFHTVFGVAGLSLMG 298
Cdd:COG5029 185 RIgEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQlPD--GGFEGAPWDGVeDVEYTFYGVGALALLG 253
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
3-280 5.75e-17

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 79.38  E-value: 5.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    3 GSLTLLKEKHIRYIESLDTKKHNFEYWLTEHLRLNGIYWGLTALCVL--DSPEtfvKEEVISFVLSCWDDKYGAFApfpr 80
Cdd:COG1689   2 TSLRFDLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLgeEVPN---RDKTIEFLESCQDEEGGGFA---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   81 hdahLLTTLSAVQILATYDAldvlgKDRKVRLISFIRGNQLEDGSfqgdRFGEVDTRFVYTALSALSILGELTSEVvDPA 160
Cdd:COG1689  75 ----LYTTSYGLMALALLGI-----DPPDEQEALEYLSDALPTKF----AGGASDLEETYLAVALLEALGASEPER-EKI 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  161 VDFVLKCYNFDGGFGLCPnaeSHAAQAFTclgALAIANKLDMLSDDQlEEIGWWLCERQLPEGGLNGRPSKLPDVCYSWW 240
Cdd:COG1689 141 REFLLSLRRPDGGFGGKK---PNLEDTYW---ALAALRRLGRDLPPA-DRVIAFILACQNEDGGFSKTPGSYSDLEATYY 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 6325434  241 VLSSLAIIGRlDWINYEKLTEFILKCQdEKKGGISDRPEN 280
Cdd:COG1689 214 ALRALKLLGE-PPKNVDKLLEFIASCQ-NSDGGFRRSPEG 251
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 100-252 2.05e-13

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 68.96  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  100 ALDVLGKD--RKVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILGELTSEVVDPAVDFVLKCYNFDGGFGLC 177
Cdd:COG5029 104 LAELLGRPppDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALDDPIETKVIRFLRDVQSPEGGFAYN 183

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325434  178 P-NAESHAAQAFTCLGALAIANKLDMLSDDQLeeigWWLCERQLPEGGLNGRP-SKLPDVCYSWWVLSSLAIIGRLD 252
Cdd:COG5029 184 TrIGEADLLSTFTAILTLYDLGAAPKLVDDLQ----AYILSLQLPDGGFEGAPwDGVEDVEYTFYGVGALALLGALA 256
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
209-249 4.42e-12

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 59.83  E-value: 4.42e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 6325434    209 EEIGWWLCERQLPEGGLNGRPSKLPDVCYSWWVLSSLAIIG 249
Cdd:pfam00432   4 EKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
254-298 1.41e-10

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 55.60  E-value: 1.41e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6325434    254 INYEKLTEFILKCQDEKkGGISDRPENEVDVFHTVFGVAGLSLMG 298
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALLG 44
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
155-198 1.81e-10

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 55.21  E-value: 1.81e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 6325434    155 EVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQAFTCLGALAIAN 198
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 40-201 2.11e-09

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 57.41  E-value: 2.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   40 YWGLTALCVLDSPETfVKEEVISFVLSCWDDKyGAFAPFPRHDAHLLTTLSAVQILatyDALDVLGKDRKVRLISFIRGN 119
Cdd:COG5029  99 YLATLLAELLGRPPP-DPDRLVRFLISQQNDD-GGFEISPGRRSDTNPTAAAIGAL---RALGALDDPIETKVIRFLRDV 173

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  120 QLEDGSFQ-GDRFGEVDTRFVYTALSALSILGElTSEVVDPAVDFVLKCYNFDGGFGLCPNAESHAAQA-FTCLGALAIA 197
Cdd:COG5029 174 QSPEGGFAyNTRIGEADLLSTFTAILTLYDLGA-APKLVDDLQAYILSLQLPDGGFEGAPWDGVEDVEYtFYGVGALALL 252


                ....
gi 6325434  198 NKLD 201
Cdd:COG5029 253 GALA 256
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
107-150 4.17e-09

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 51.36  E-value: 4.17e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 6325434    107 DRKVRLISFIRGNQLEDGSFQGDRFGEVDTRFVYTALSALSILG 150
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 152-306 2.98e-07

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 50.86  E-value: 2.98e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  152 LTSEVVDPAVDFVLKCYNFDGGFGlCPNAESHAAQAFTCLGALAIANKLDMLSDDQLEeigwWLCERQLPEGGLNGRPSK 231
Cdd:COG5029  16 STADFTDSHLDYLRASQNPDGGFA-GRSGPSDLYSTYYAVRTLALLGESPKWRDRVAD----LLSSLRVEDGGFAKAPEG 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6325434  232 LPDVCY-SWWVLSSLAIIGRLDWINyEKLTEFILKCQDEkKGGISDRPENEVDVFHTVFGVAGLSLMGYDNlVPID 306
Cdd:COG5029  91 GAGSTYhTYLATLLAELLGRPPPDP-DRLVRFLISQQND-DGGFEISPGRRSDTNPTAAAIGALRALGALD-DPIE 163
SQCY cd02889
Squalene cyclase (SQCY) domain; found in class II terpene cyclases that have an alpha 6 - ...
 77-223 8.11e-06

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: 46.83  E-value: 8.11e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   77 PFPRHDAHLLTTLSAVQILATYDALDVlgKDRKVRLISFIRGNQLEDGSFQGdRFGevdTRFVY---TALSALSILGE-L 152
Cdd:cd02889 163 PYVECTGSVLEALGLFGKLYPEHRREI--DPAIRRAVKYLEREQEPDGSWYG-RWG---VCFIYgtwFALEALAAAGEdE 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  153 TSEVVDPAVDFVLKCYNFDGGFG----LCPN---AESHAAQAF-TCLGALAiankLDMLSDDQLEEI--GW-WLCERQLP 221
Cdd:cd02889 237 NSPYVRKACDWLLSKQNPDGGWGesyeSYEDpsyAGGGRSTVVqTAWALLA----LMAAGEPDSEAVkrGVkYLLNTQQE 312


                ..
gi 6325434  222 EG 223
Cdd:cd02889 313 DG 314
SQCY_1 cd02892
Squalene cyclase (SQCY) domain subgroup 1; found in class II terpene cyclases that have an ...
 83-175 1.19e-05

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: 46.81  E-value: 1.19e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   83 AHLLTTLSAVQILATYDALDVlgKDRKVRLISFIRGNQLEDGSFQGdRFGevdTRFVY---TALSALSILGE--LTSEVV 157
Cdd:cd02892 454 GSVLEALGLFGKLYPGHRREI--DPAIRRAVKYLLREQEPDGSWYG-RWG---VCYIYgtwFALEALAAAGEdyENSPYI 527

                        90
                ....*....|....*...
gi 6325434  158 DPAVDFVLKCYNFDGGFG 175
Cdd:cd02892 528 RKACDFLLSKQNPDGGWG 545
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 216-306 1.48e-05

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


Pssm-ID: 239220 [Multi-domain]  Cd Length: 286  Bit Score: 45.65  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434  216 CERQLPEGGLNGRPSKLpdvCYSWWVLSSLAIIGR-LDWINYEKLTEFILKCQDEKKGGISDRPENEVDVFHTVFGVAGL 294
Cdd:cd02890  11 CLKLLPSSYTSLDASRL---WLLYWILSSLDLLGEdLDDENKDEIIDFIYSCQVNEDGGFGGGPGQDPHLASTYAAVLSL 87

                        90
                ....*....|..
gi 6325434  295 SLMGYDNLVPID 306
Cdd:cd02890  88 AILGDDALSRID 99
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
55-99 2.89e-04

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 37.88  E-value: 2.89e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 6325434     55 FVKEEVISFVLSCWDDkYGAFAPFPRHDAHLLTTLSAVQILATYD 99
Cdd:pfam00432   1 IDKEKLVDYLLSCQNE-DGGFGGRPGGESDTYYTYCALAALALLG 44
SqhC COG1657
Terpene cyclase SqhC [Lipid transport and metabolism];
42-223 6.61e-04

Terpene cyclase SqhC [Lipid transport and metabolism];


Pssm-ID: 441263 [Multi-domain]  Cd Length: 644  Bit Score: 41.34  E-value: 6.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   42 GLTALCVLDSPETFVKEEVIS----FVLS--CWDDKYGAF-----------APFPRHDAhlLT-------TLSAVQILAT 97
Cdd:COG1657 396 VLMALLRLRLPDEPRYREAIEraveWILGmqSRDGGWGAFdkdntkewlnkIPFADHGA--LLdpptadvTARCLEMLGQ 473

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434   98 YDaldvLGKDRKV--RLISFIRGNQLEDGSFQGdRFGevdTRFVY---TALSALSILGELTSevvDP----AVDFVLKCY 168
Cdd:COG1657 474 LG----LTEDHPAirRAVAYLRREQEPDGSWFG-RWG---VNYIYgtwSVLTGLNAAGVDPD---DPairrAVAWLLSIQ 542

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6325434  169 NFDGGFG----------LCPNAESHAAQ-AFTCLGALAiANKLDmlsDDQLEE-IGwWLCERQLPEG 223
Cdd:COG1657 543 NADGGWGedcrsyedprYVGLGPSTASQtAWALLALLA-AGEAD---SPAVARgIA-YLLSTQREDG 604
SQHop_cyclase_C pfam13243
Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes ...
 110-224 6.79e-04

Squalene-hopene cyclase C-terminal domain; Squalene-hopene cyclase, EC:5.4.99.17, catalyzes the cyclization of squalene into hopene in bacteria. This reaction is part of a cationic cyclization cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the C-terminal half of the molecule.


Pssm-ID: 433057 [Multi-domain]  Cd Length: 319  Bit Score: 40.78  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    110 VRLISFIRGNQLEDGSFQGdRFGevdTRFVY---TALSALSILGELTSE-VVDPAVDFVLKCYNFDGGFGLCPN------ 179
Cdd:pfam13243 162 ARALEYLKKEQEPDGSWFG-RWG---VNYIYgtwSVLCGLAAVGEDHNRpYIRKAVDWLKSRQNPDGGWGEDCEsykdpk 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 6325434    180 ----AESHAAQ-AFTCLGALAiANKLDmlSDDQLEEIGwWLCERQLPEGG 224
Cdd:pfam13243 238 lagrGPSTASQtAWALLALMA-AGEVD--SPAVRRGIQ-YLLETQKPDGT 283
squalene_cyclas TIGR01787
squalene/oxidosqualene cyclases; This family of enzymes catalyzes the cyclization of the ...
 111-226 2.26e-03

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: 39.73  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6325434    111 RLISFIRGNQLEDGSFQGdRFGevdTRFVY---TALSALSILGELTSE--VVDPAVDFVLKCYNFDGGFG----LCPN-- 179
Cdd:TIGR01787 464 RALEYLRREQRADGSWFG-RWG---VNYTYgtgFVLSALAAAGRTYRNcpEVQKACDWLLSRQMPDGGWGedcfSYEDps 539

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 6325434    180 -AESHAAQAF-TCLGALAIANKLDMLSDDQLEEIGwWLCERQLPEGGLN 226
Cdd:TIGR01787 540 yVGSGGSTPSqTGWALMALIAAGEADSEAIERGVK-YLLETQRPDGDWP 587
hopene_cyclase TIGR01507
squalene-hopene cyclase; SHC is an essential prokaryotic gene in hopanoid (triterpenoid) ...
 103-175 2.37e-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: 39.49  E-value: 2.37e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6325434    103 VLGKDRKV--RLISFIRGNQLEDGSFqgdrFGEVDTRFVY---TALSALSILGELTSE-VVDPAVDFVLKCYNFDGGFG 175
Cdd:TIGR01507 465 GYDDAWPVieRAVEYLKREQEPDGSW----FGRWGVNYLYgtgAVLSALKAVGIDTREpYIQKALAWLESHQNPDGGWG 539
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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