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Conserved domains on  [gi|21355687|ref|NP_650540|]
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farnesyl transferase beta subunit [Drosophila melanogaster]

Protein Classification

protein farnesyltransferase subunit beta( domain architecture ID 10121010)

protein farnesyltransferase subunit beta is an essential subunit of the farnesyltransferase complex that catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 62-360 2.85e-173

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: 485.97  E-value: 2.85e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  62 RLEHQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLLSFNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTY 141
Cdd:cd02893   1 REKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 142 AAVNSLCIIGSEQAYRAIDRPTLVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPvikELFAGTGDWIAQ 221
Cdd:cd02893  81 AAVNALAIIGTEEAYDVIDREALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTD---ELFEGVAEYILS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 222 CQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQALLKWTLRRQMTYEGGFQGRTNKLVDGCYSFWVGATIPIT 301
Cdd:cd02893 158 CQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLRWLVARQMRFEGGFQGRTNKLVDGCYSFWVGGSLPIL 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355687 302 QATLSGVDK---QMEHTLFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIA 360
Cdd:cd02893 238 EAILNAEKKfddSAEGTLFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHTCYALSGLSIA 299
 
Name Accession Description Interval E-value
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 62-360 2.85e-173

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: 485.97  E-value: 2.85e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  62 RLEHQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLLSFNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTY 141
Cdd:cd02893   1 REKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 142 AAVNSLCIIGSEQAYRAIDRPTLVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPvikELFAGTGDWIAQ 221
Cdd:cd02893  81 AAVNALAIIGTEEAYDVIDREALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTD---ELFEGVAEYILS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 222 CQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQALLKWTLRRQMTYEGGFQGRTNKLVDGCYSFWVGATIPIT 301
Cdd:cd02893 158 CQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLRWLVARQMRFEGGFQGRTNKLVDGCYSFWVGGSLPIL 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355687 302 QATLSGVDK---QMEHTLFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIA 360
Cdd:cd02893 238 EAILNAEKKfddSAEGTLFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHTCYALSGLSIA 299
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 27-403 2.71e-127

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 374.51  E-value: 2.71e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687   27 TTTSREQQKTESSVEKCFDrfeqIMFTDPRLTQIFRLE-----HQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLL 101
Cdd:PLN02710  10 TVTQREQWKVEAKVFDIYR----SFASAPPNAQSVMLElwrekHLEYLTRGLRQLGPSFSVLDANRPWLCYWILHSIALL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  102 SFNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTYAAVNSLCIIGSEQAYRAIDRPTLVQFLFSVRDSDGSFRLH 181
Cdd:PLN02710  86 GESLDDELENDTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLVTIGGERALSSINREKLYTFLLRMKDPSGGFRMH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  182 VDGETDVRGAYCAISCAKLLNLPEPvikELFAGTGDWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQ 261
Cdd:PLN02710 166 DGGEMDVRACYTAISVASLLNILDD---ELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLP 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  262 ALLKWTLRRQMTyEGGFQGRTNKLVDGCYSFWVGATIPITQATLSGVDKQMEHT-------------------------- 315
Cdd:PLN02710 243 SLINWVVFRQGV-EGGFQGRTNKLVDGCYSFWQGGVFALLQQLVTIVDEQLQTGgssimfeeleddacetsssgkddagd 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  316 -----------------------LFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIAQHS------ECA 366
Cdd:PLN02710 322 tdsadyskvgfdfikasnqqmgpLFHSIALQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLSVAQYSaskdedSPP 401

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 21355687  367 SSPQVLGDTINELLPTHPLFNIPPKSVAAARSHFSNS 403
Cdd:PLN02710 402 LPRHVLGPYSNLLEPIHPLYNVVLDKYHEAIEFFSSK 438
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 94-361 6.24e-14

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 71.28  E-value: 6.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  94 ILQAAQLLSFNFDDQTLNhvvqFLSNCRSPTGGFGGGPGqYAHLAPTYAAVNSLCIIGSEQAYRaiDRPtlVQFLFSVRD 173
Cdd:COG5029   9 LEGGSSKSTADFTDSHLD----YLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR--DRV--ADLLSSLRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 174 SDGSFRLHVDGETD-VRGAYCAISCAKLLNLPEPVIKELFAgtgdWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALL 252
Cdd:COG5029  80 EDGGFAKAPEGGAGsTYHTYLATLLAELLGRPPPDPDRLVR----FLISQQNDDGGFEISPGRRSDTNPTAAAIGALRAL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 253 NEADKCDRQALLKWTLRRQMTyEGGFQ-GRTNKLVDGCYSFWVGATIpitqatlsgvdKQMEHTLFDVEALQEYIlLCCQ 331
Cdd:COG5029 156 GALDDPIETKVIRFLRDVQSP-EGGFAyNTRIGEADLLSTFTAILTL-----------YDLGAAPKLVDDLQAYI-LSLQ 222

                       250       260       270
                ....*....|....*....|....*....|.
gi 21355687 332 KQSGGLIDKPGKPQ-DLYHTCYTLSGVSIAQ 361
Cdd:COG5029 223 LPDGGFEGAPWDGVeDVEYTFYGVGALALLG 253
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
217-253 3.83e-09

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 52.13  E-value: 3.83e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 21355687   217 DWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLN 253
Cdd:pfam00432   8 DYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
 
Name Accession Description Interval E-value
FTase cd02893
Protein farnesyltransferase (FTase)_like proteins containing the protein prenyltransferase ...
 62-360 2.85e-173

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: 485.97  E-value: 2.85e-173
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  62 RLEHQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLLSFNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTY 141
Cdd:cd02893   1 REKHIKYLKKSLRQLPSSFTSLDASRPWLLYWILHSLELLGEELDQSYADDVISFLRRCQNPSGGFGGGPGQLPHLATTY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 142 AAVNSLCIIGSEQAYRAIDRPTLVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPvikELFAGTGDWIAQ 221
Cdd:cd02893  81 AAVNALAIIGTEEAYDVIDREALYKFLLSLKQPDGSFRMHVGGEVDVRGTYCAISVASLLNILTD---ELFEGVAEYILS 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 222 CQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQALLKWTLRRQMTYEGGFQGRTNKLVDGCYSFWVGATIPIT 301
Cdd:cd02893 158 CQTYEGGFGGVPGNEAHGGYTFCALAALAILGKPDKLDLESLLRWLVARQMRFEGGFQGRTNKLVDGCYSFWVGGSLPIL 237

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355687 302 QATLSGVDK---QMEHTLFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIA 360
Cdd:cd02893 238 EAILNAEKKfddSAEGTLFDQEALQEYILLCCQSEEGGLRDKPGKPRDFYHTCYALSGLSIA 299
PTase cd02890
Protein prenyltransferase (PTase) domain, beta subunit (alpha 6 - alpha 6 barrel fold). The ...
 65-360 7.65e-129

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: 372.69  E-value: 7.65e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  65 HQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLLSFNFDDQTLNHVVQFLSNC-RSPTGGFGGGPGQYAHLAPTYAA 143
Cdd:cd02890   4 HIKYLQRCLKLLPSSYTSLDASRLWLLYWILSSLDLLGEDLDDENKDEIIDFIYSCqVNEDGGFGGGPGQDPHLASTYAA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 144 VNSLCIIGSEqAYRAIDRPTLVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPVIKElfaGTGDWIAQCQ 223
Cdd:cd02890  84 VLSLAILGDD-ALSRIDREKIYKFLSSLQNPDGSFRGDLGGEVDTRFVYCALSILSLLNILTDIDKE---KLIDYILSCQ 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 224 TYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQALLKWTLRRQMTYEGGFQGRTNKLVDGCYSFWVGATIPITQA 303
Cdd:cd02890 160 NYDGGFGGVPGAESHGGYTFCAVASLALLGRLDLIDKERLLRWLVERQLASGGGFNGRPNKLVDTCYSFWVGASLKILGR 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 21355687 304 TlsgvdkqmehTLFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIA 360
Cdd:cd02890 240 L----------HLIDQEKLREYILSCQQSEVGGFSDKPGKPPDLYHTYYGLSGLSLL 286
PLN02710 PLN02710
farnesyltranstransferase subunit beta
 27-403 2.71e-127

farnesyltranstransferase subunit beta


Pssm-ID: 215380 [Multi-domain]  Cd Length: 439  Bit Score: 374.51  E-value: 2.71e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687   27 TTTSREQQKTESSVEKCFDrfeqIMFTDPRLTQIFRLE-----HQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLL 101
Cdd:PLN02710  10 TVTQREQWKVEAKVFDIYR----SFASAPPNAQSVMLElwrekHLEYLTRGLRQLGPSFSVLDANRPWLCYWILHSIALL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  102 SFNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTYAAVNSLCIIGSEQAYRAIDRPTLVQFLFSVRDSDGSFRLH 181
Cdd:PLN02710  86 GESLDDELENDTIDFLSRCQDPNGGYGGGPGQLPHLATTYAAVNTLVTIGGERALSSINREKLYTFLLRMKDPSGGFRMH 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  182 VDGETDVRGAYCAISCAKLLNLPEPvikELFAGTGDWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQ 261
Cdd:PLN02710 166 DGGEMDVRACYTAISVASLLNILDD---ELVKGVGDYILSCQTYEGGIGGEPGAEAHGGYTFCGLAAMILINEVDRLDLP 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  262 ALLKWTLRRQMTyEGGFQGRTNKLVDGCYSFWVGATIPITQATLSGVDKQMEHT-------------------------- 315
Cdd:PLN02710 243 SLINWVVFRQGV-EGGFQGRTNKLVDGCYSFWQGGVFALLQQLVTIVDEQLQTGgssimfeeleddacetsssgkddagd 321

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  316 -----------------------LFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIAQHS------ECA 366
Cdd:PLN02710 322 tdsadyskvgfdfikasnqqmgpLFHSIALQQYILLCSQVLDGGLRDKPGKSRDYYHTCYCLSGLSVAQYSaskdedSPP 401

                        410       420       430
                 ....*....|....*....|....*....|....*..
gi 21355687  367 SSPQVLGDTINELLPTHPLFNIPPKSVAAARSHFSNS 403
Cdd:PLN02710 402 LPRHVLGPYSNLLEPIHPLYNVVLDKYHEAIEFFSSK 438
ISOPREN_C2_like cd00688
This group contains class II terpene cyclases, protein prenyltransferases beta subunit, two ...
 62-360 5.39e-58

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: 192.00  E-value: 5.39e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  62 RLEHQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLLSFNF-----DDQTLNHVVQFLSNCRSPTGG-FGGGPGQYA 135
Cdd:cd00688   1 IEKHLKYLLRYPYGDGHWYQSLCGEQTWSTAWPLLALLLLLAATgirdkADENIEKGIQRLLSYQLSDGGfSGWGGNDYP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 136 HLAPTYAAVNSLCIIGSEQAYRAIDRPTLVQFLFSVRDSDGSFRLHVDG-------ETDVRGAYCAISCAKLLNLPEPvi 208
Cdd:cd00688  81 SLWLTAYALKALLLAGDYIAVDRIDLARALNWLLSLQNEDGGFREDGPGnhriggdESDVRLTAYALIALALLGKLDP-- 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 209 KELFAGTGDWIAQCQTYEGGFGgaPGLEAHGGYTFCGIAGLALLNEADKCDRQALLKWTLRRQMTYEGGFQGR--TNKLV 286
Cdd:cd00688 159 DPLIEKALDYLLSCQNYDGGFG--PGGESHGYGTACAAAALALLGDLDSPDAKKALRWLLSRQRPDGGWGEGRdrTNKLS 236

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21355687 287 DGCYSFWVGATIPITQATlsgvdkqmeHTLFDVEALQEYILLcCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIA 360
Cdd:cd00688 237 DSCYTEWAAYALLALGKL---------GDLEDAEKLVKWLLS-QQNEDGGFSSKPGKSYDTQHTVFALLALSLY 300
GGTase-I cd02895
Geranylgeranyltransferase types I (GGTase-I)-like proteins containing the protein ...
 65-359 6.15e-58

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: 192.11  E-value: 6.15e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  65 HQYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLL-SFNFDDQ-----TLNHVV--QFLSN------CRSPTGGFGGG 130
Cdd:cd02895   4 HVKFFQRCLQLLPSSYQSLDTNRLTIAFFALSGLDLLgALDSILVeekddIIEWIYslQVLSNlprggfRGSSTLGLPGT 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 131 PGQY--AHLAPTYAAVNSLCIIGSEqaYRAIDRPTLVQFLFSVRDSDGSFR---LHVDGETDVRGAYCAISCAKLLN--L 203
Cdd:cd02895  84 ASKYdtGNLAMTYFALLSLLILGDD--LSRVDRKAILNFLSKLQLPDGSFGsvlDSEGGENDMRFCYCAVAICYMLDdwS 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 204 PEPVIKE-LFagtgDWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCD---RQALLKWTLRRQMTYeGGFQ 279
Cdd:cd02895 162 EEDIDKEkLI----DYIKSSQSYDGGFGQGPGLESHGGSTFCAIASLSLLGKLEELSekfLERLKRWLVHRQVSG-TGFN 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 280 GRTNKLVDGCYSFWVGATIPITQAtlsgvdkqmeHTLFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSI 359
Cdd:cd02895 237 GRPNKPADTCYSFWVGASLKLLDA----------FQLIDFEKNRNYLLSTQQSLVGGFAKNPDSHPDPLHSYLGLAALSL 306
GGTase-II cd02894
Geranylgeranyltransferase type II (GGTase-II)_like proteins containing the protein ...
 66-358 1.28e-48

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


Pssm-ID: 239224 [Multi-domain]  Cd Length: 287  Bit Score: 167.06  E-value: 1.28e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  66 QYYLDAMLRRLPSNYECLDSSRAWCVYWILQAAQLLsFNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQY-AHLAPTYAAV 144
Cdd:cd02894   8 EYILSLTKKKDDYEYILTEHLRMSGIYWGLTALDLL-GQLERLNREEIIEFVKSCQDNEDGGFGGSPGHdPHILSTLSAI 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 145 NSLCIIGseqAYRAIDRP--TLVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPVIKElfaGTGDWIAQC 222
Cdd:cd02894  87 QILALYD---LLNKIDENkeKIAKFIKGLQNEDGSFSGDKWGEVDTRFSYCAVLCLTLLGKLDLIDVD---KAVDYLLSC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 223 QTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCDRQALLKWTLRRQmTYEGGFQGRTNKLVDGCYSFWVGatipitq 302
Cdd:cd02894 161 YNFDGGFGCRPGAESHAGQIFCCVGALAILGSLDLIDRDRLGWWLCERQ-LPSGGLNGRPEKLPDVCYSWWVL------- 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355687 303 ATLSGVDKQMehtLFDVEALQEYILLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVS 358
Cdd:cd02894 233 SSLKIIGRLH---WINKNKLKNFILACQDEEDGGFADRPGNMVDVFHTFFGLAGLS 285
PLN03201 PLN03201
RAB geranylgeranyl transferase beta-subunit; Provisional
 91-362 5.92e-40

RAB geranylgeranyl transferase beta-subunit; Provisional


Pssm-ID: 215630 [Multi-domain]  Cd Length: 316  Bit Score: 144.84  E-value: 5.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687   91 VYWILQAAQLLSfNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTYAAVNSLCIIgseQAYRAIDRPTLVQFLFS 170
Cdd:PLN03201  40 AYWGLTALDLLG-KLDDVDRDEVVSWVMRCQHESGGFGGNTGHDPHILYTLSAVQILALF---DRLDLLDADKVASYVAG 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  171 VRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPVIKELFAgtgDWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLA 250
Cdd:PLN03201 116 LQNEDGSFSGDEWGEIDTRFSYCALCCLSLLKRLDKINVEKAV---DYIVSCKNFDGGFGCTPGGESHAGQIFCCVGALA 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  251 LLNEADKCDRQALLKWTLRRQmTYEGGFQGRTNKLVDGCYSFWVgatipitQATLSGVDKQmeHTLfDVEALQEYILLCC 330
Cdd:PLN03201 193 ITGSLHHVDKDLLGWWLCERQ-VKSGGLNGRPEKLPDVCYSWWV-------LSSLIIIDRV--HWI-DKDKLAKFILDCQ 261

                        250       260       270
                 ....*....|....*....|....*....|..
gi 21355687  331 QKQSGGLIDKPGKPQDLYHTCYTLSGVSIAQH 362
Cdd:PLN03201 262 DDENGGISDRPDDAVDVFHTFFGVAGLSLLGY 293
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 94-361 6.24e-14

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 71.28  E-value: 6.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  94 ILQAAQLLSFNFDDQTLNhvvqFLSNCRSPTGGFGGGPGqYAHLAPTYAAVNSLCIIGSEQAYRaiDRPtlVQFLFSVRD 173
Cdd:COG5029   9 LEGGSSKSTADFTDSHLD----YLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPKWR--DRV--ADLLSSLRV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 174 SDGSFRLHVDGETD-VRGAYCAISCAKLLNLPEPVIKELFAgtgdWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALL 252
Cdd:COG5029  80 EDGGFAKAPEGGAGsTYHTYLATLLAELLGRPPPDPDRLVR----FLISQQNDDGGFEISPGRRSDTNPTAAAIGALRAL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 253 NEADKCDRQALLKWTLRRQMTyEGGFQ-GRTNKLVDGCYSFWVGATIpitqatlsgvdKQMEHTLFDVEALQEYIlLCCQ 331
Cdd:COG5029 156 GALDDPIETKVIRFLRDVQSP-EGGFAyNTRIGEADLLSTFTAILTL-----------YDLGAAPKLVDDLQAYI-LSLQ 222

                       250       260       270
                ....*....|....*....|....*....|.
gi 21355687 332 KQSGGLIDKPGKPQ-DLYHTCYTLSGVSIAQ 361
Cdd:COG5029 223 LPDGGFEGAPWDGVeDVEYTFYGVGALALLG 253
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 88-252 1.78e-11

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


Pssm-ID: 444045 [Multi-domain]  Cd Length: 259  Bit Score: 63.96  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  88 AWCVYWILQAAQLLsfNFDDQTLNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTYAAVNSLCIIGseqAYRAIDRPTLVQF 167
Cdd:COG5029  95 TYHTYLATLLAELL--GRPPPDPDRLVRFLISQQNDDGGFEISPGRRSDTNPTAAAIGALRALG---ALDDPIETKVIRF 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 168 LFSVRDSDGSFRLHVD-GETDVRGAYCAISCAKLLNLPEpvikELFAGTGDWIAQCQTYEGGFGGAPGlEAHG--GYTFC 244
Cdd:COG5029 170 LRDVQSPEGGFAYNTRiGEADLLSTFTAILTLYDLGAAP----KLVDDLQAYILSLQLPDGGFEGAPW-DGVEdvEYTFY 244


                ....*...
gi 21355687 245 GIAGLALL 252
Cdd:COG5029 245 GVGALALL 252
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
217-253 3.83e-09

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 52.13  E-value: 3.83e-09
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 21355687   217 DWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLN 253
Cdd:pfam00432   8 DYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
136-252 2.09e-07

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 52.03  E-value: 2.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 136 HLAPTYAAVNSLCIIGseqayRAIDRPT-LVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLNLPEPVIKELFag 214
Cdd:COG1689 160 NLEDTYWALAALRRLG-----RDLPPADrVIAFILACQNEDGGFSKTPGSYSDLEATYYALRALKLLGEPPKNVDKLL-- 232

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 21355687 215 tgDWIAQCQTYEGGFGGAPgleaHGG-----YTFCGIAGLALL 252
Cdd:COG1689 233 --EFIASCQNSDGGFRRSP----EGGistleYTYYALAVLKWL 269
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
159-202 4.14e-07

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 46.35  E-value: 4.14e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 21355687   159 IDRPTLVQFLFSVRDSDGSFRLHVDGETDVRGAYCAISCAKLLN 202
Cdd:pfam00432   1 IDKEKLVDYLLSCQNEDGGFGGRPGGESDTYYTYCALAALALLG 44
CAL1 COG5029
Prenyltransferase, beta subunit [Posttranslational modification, protein turnover, chaperones, ...
 217-364 4.76e-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: 4.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 217 DWIAQCQTYEGGFGGAPGlEAHGGYTFCGIAGLALLNEADKcDRQALLKW--TLRRQmtyEGGFQGRTNKLVDGCY-SFW 293
Cdd:COG5029  26 DYLRASQNPDGGFAGRSG-PSDLYSTYYAVRTLALLGESPK-WRDRVADLlsSLRVE---DGGFAKAPEGGAGSTYhTYL 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355687 294 vgatipitqATLSGVdkQMEHTLFDVEALQEYiLLCCQKQSGGLIDKPGKPQDLYHTCYTLSGVSIAQHSE 364
Cdd:COG5029 101 ---------ATLLAE--LLGRPPPDPDRLVRF-LISQQNDDGGFEISPGRRSDTNPTAAAIGALRALGALD 159
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
259-297 9.01e-06

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 42.50  E-value: 9.01e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 21355687   259 DRQALLKWTLRRQMtYEGGFQGRTNKLVDGCYSFWVGAT 297
Cdd:pfam00432   2 DKEKLVDYLLSCQN-EDGGFGGRPGGESDTYYTYCALAA 39
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
136-278 1.92e-05

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 45.87  E-value: 1.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 136 HLAPTYAAVNSLCIIGSEqayrAIDRPTLVQFLFSVRDSDGSFRLhvdGETDVRGAYCAISCAKLLNLPEPVIKELFagt 215
Cdd:COG1689 116 DLEETYLAVALLEALGAS----EPEREKIREFLLSLRRPDGGFGG---KKPNLEDTYWALAALRRLGRDLPPADRVI--- 185

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355687 216 gDWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKCdRQALLKWTLRRQMTyEGGF 278
Cdd:COG1689 186 -AFILACQNEDGGFSKTPGSYSDLEATYYALRALKLLGEPPKN-VDKLLEFIASCQNS-DGGF 245
Prenyltrans pfam00432
Prenyltransferase and squalene oxidase repeat;
317-360 8.29e-05

Prenyltransferase and squalene oxidase repeat;


Pssm-ID: 395346 [Multi-domain]  Cd Length: 44  Bit Score: 39.80  E-value: 8.29e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 21355687   317 FDVEALQEYILLCCQKQsGGLIDKPGKPQDLYHTCYTLSGVSIA 360
Cdd:pfam00432   1 IDKEKLVDYLLSCQNED-GGFGGRPGGESDTYYTYCALAALALL 43
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
110-336 1.51e-04

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 43.17  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 110 LNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTYAAVNSLCIIGSEQAyraiDRPTLVQFLFSVRDSDG--------SFRLH 181
Cdd:COG1689   8 LARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLGEEVP----NRDKTIEFLESCQDEEGggfalyttSYGLM 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 182 V---------------------------DGETDVRGAYCAISCAKLLNLPEPVIKELFAgtgdWIAQCQTYEGGFGG-AP 233
Cdd:COG1689  84 AlallgidppdeqealeylsdalptkfaGGASDLEETYLAVALLEALGASEPEREKIRE----FLLSLRRPDGGFGGkKP 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 234 GLEAHGGYtfcgiagLALLNEADK--CDRQALLKWTLRRQmTYEGGFQgrtnklvdgcysfWVGATIPITQATLSGVdKQ 311
Cdd:COG1689 160 NLEDTYWA-------LAALRRLGRdlPPADRVIAFILACQ-NEDGGFS-------------KTPGSYSDLEATYYAL-RA 217

                       250       260
                ....*....|....*....|....*...
gi 21355687 312 MEH---TLFDVEALQEYILLcCQKQSGG 336
Cdd:COG1689 218 LKLlgePPKNVDKLLEFIAS-CQNSDGG 244
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
211-314 5.92e-04

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 41.25  E-value: 5.92e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687 211 LFAGTGDWIAQCQTYEGGFGGAPGLEAHGGYTFCGIAGLALLNEADKcDRQALLKWtLRRQMTYEGGFQGRTNkLVDGCY 290
Cdd:COG1689   7 DLARTIEYVLKRQNEDGGFCAYPGLPSTLADTYYAVRILKLLGEEVP-NRDKTIEF-LESCQDEEGGGFALYT-TSYGLM 83

                        90       100
                ....*....|....*....|....*
gi 21355687 291 SF-WVGATIPITQATLSGVDKQMEH 314
Cdd:COG1689  84 ALaLLGIDPPDEQEALEYLSDALPT 108
AF1543 COG1689
Class II terpene cyclase family protein AF1543 [General function prediction only];
92-179 7.06e-03

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


Pssm-ID: 441295 [Multi-domain]  Cd Length: 272  Bit Score: 38.17  E-value: 7.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355687  92 YWILQAAQLLSFNFDDQtlNHVVQFLSNCRSPTGGFGGGPGQYAHLAPTYAAVNSLCIIGSeqayRAIDRPTLVQFLFSV 171
Cdd:COG1689 165 YWALAALRRLGRDLPPA--DRVIAFILACQNEDGGFSKTPGSYSDLEATYYALRALKLLGE----PPKNVDKLLEFIASC 238


                ....*...
gi 21355687 172 RDSDGSFR 179
Cdd:COG1689 239 QNSDGGFR 246
 
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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