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Conserved domains on  [gi|219118556|ref|XP_002180048|]
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predicted protein [Phaeodactylum tricornutum CCAP 1055/1]

Protein Classification

protein prenyltransferase subunit alpha family protein( domain architecture ID 11477143)

protein prenyltransferase subunit alpha family protein such as Homo sapiens GGTase-I-alpha, which contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl 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
PLN02789 PLN02789
farnesyltranstransferase
1-331 1.30e-148

farnesyltranstransferase


:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 420.69  E-value: 1.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556   1 MPLTTIDLPTVFADLAPIPQQDGPHAVCRIDYPPDFTLAYDYMRALWKADERSRRALDLTTLCLELNPANYTVWHFRRLC 80
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  81 LEALNlrndqTQIGVDLALAADLGGSNPKNYQIWYHRRALLEKLDNpkilrDYCHQELSYIASVIVKDGKNYHAWSHRQW 160
Cdd:PLN02789  81 LEALD-----ADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGP-----DAANKELEFTRKILSLDAKNYHAWSHRQW 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 161 ILRTLNDdtaWTDEVLYTEYLIDEDLRNNSAWNGRWFAVHRGQKeLLSVETDGPAQADYAIKIARLDPYNESPWRFLIAV 240
Cdd:PLN02789 151 VLRTLGG---WEDELEYCHQLLEEDVRNNSAWNQRYFVITRSPL-LGGLEAMRDSELKYTIDAILANPRNESPWRYLRGL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 241 LNEQrpqlshdqfielvesylgrileIQENVVEPSGKGPCPNLLSAQVD-------LLEWMSDGSSKTK----------- 302
Cdd:PLN02789 227 FKDD----------------------KEALVSDPEVSSVCLEVLSKDSNhvfalsdLLDLLCEGLQPTAefrdtvdtlae 284
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 219118556 303 -------ALDYLEELKTHDPIRKRYWAMRQQQIQAL 331
Cdd:PLN02789 285 elsdstlAQAVCSELEVADPMRRNYWAWRKSKLPKA 320
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
1-331 1.30e-148

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 420.69  E-value: 1.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556   1 MPLTTIDLPTVFADLAPIPQQDGPHAVCRIDYPPDFTLAYDYMRALWKADERSRRALDLTTLCLELNPANYTVWHFRRLC 80
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  81 LEALNlrndqTQIGVDLALAADLGGSNPKNYQIWYHRRALLEKLDNpkilrDYCHQELSYIASVIVKDGKNYHAWSHRQW 160
Cdd:PLN02789  81 LEALD-----ADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGP-----DAANKELEFTRKILSLDAKNYHAWSHRQW 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 161 ILRTLNDdtaWTDEVLYTEYLIDEDLRNNSAWNGRWFAVHRGQKeLLSVETDGPAQADYAIKIARLDPYNESPWRFLIAV 240
Cdd:PLN02789 151 VLRTLGG---WEDELEYCHQLLEEDVRNNSAWNQRYFVITRSPL-LGGLEAMRDSELKYTIDAILANPRNESPWRYLRGL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 241 LNEQrpqlshdqfielvesylgrileIQENVVEPSGKGPCPNLLSAQVD-------LLEWMSDGSSKTK----------- 302
Cdd:PLN02789 227 FKDD----------------------KEALVSDPEVSSVCLEVLSKDSNhvfalsdLLDLLCEGLQPTAefrdtvdtlae 284
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 219118556 303 -------ALDYLEELKTHDPIRKRYWAMRQQQIQAL 331
Cdd:PLN02789 285 elsdstlAQAVCSELEVADPMRRNYWAWRKSKLPKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
12-328 7.06e-32

Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 121.52  E-value: 7.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  12 FADLAPIPQQ-DGPHAVCRIDYPPDFTLAYDYMRALWKADERSRRALDLTTLCLELNPANYTVWHFRRLCLEALNLRNDQ 90
Cdd:COG5536    6 LRRVKPLPIQfDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSED 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  91 TQIGVD--LALAADLGGSNPKNYQIWYHRRALLEKLDNPKILRdychqELSYIASVIVKDGKNYHAWSHRQWILRTLNDD 168
Cdd:COG5536   86 KEHLLDneLDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGR-----ELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 169 TAWTD---EVLYTEYLIDEDLRNNSAWNGR--WFAVHRGQKELLSvETDGPAQADYAIKIARLDPYNESPWRFLIAVLNE 243
Cdd:COG5536  161 FNFSDlkhELEYTTSLIETDIYNNSAWHHRyiWIERRFNRGDVIS-QKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 244 qrPQLSHDQFIELVESYLGRILEIQENVVEPSGK---GPCPNLLSAQVDLLEW---MSDGSSKTKAldYLEELKTHDPIR 317
Cdd:COG5536  240 --FATDIVMIGEKVEDLGKYIVIINGKELDLGPKenlPCLHSLLELEFLCHAEkalLTERDIEQKA--LVELAIKVDPAR 315
                        330
                 ....*....|.
gi 219118556 318 KRYWAMRQQQI 328
Cdd:COG5536  316 RNLYSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
135-165 2.14e-05

Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognize a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognizes a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family.


Pssm-ID: 460128 [Multi-domain]  Cd Length: 32  Bit Score: 40.70  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 219118556  135 HQELSYIASVIVKDGKNYHAWSHRQWILRTL 165
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
1-331 1.30e-148

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 420.69  E-value: 1.30e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556   1 MPLTTIDLPTVFADLAPIPQQDGPHAVCRIDYPPDFTLAYDYMRALWKADERSRRALDLTTLCLELNPANYTVWHFRRLC 80
Cdd:PLN02789   1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  81 LEALNlrndqTQIGVDLALAADLGGSNPKNYQIWYHRRALLEKLDNpkilrDYCHQELSYIASVIVKDGKNYHAWSHRQW 160
Cdd:PLN02789  81 LEALD-----ADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGP-----DAANKELEFTRKILSLDAKNYHAWSHRQW 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 161 ILRTLNDdtaWTDEVLYTEYLIDEDLRNNSAWNGRWFAVHRGQKeLLSVETDGPAQADYAIKIARLDPYNESPWRFLIAV 240
Cdd:PLN02789 151 VLRTLGG---WEDELEYCHQLLEEDVRNNSAWNQRYFVITRSPL-LGGLEAMRDSELKYTIDAILANPRNESPWRYLRGL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 241 LNEQrpqlshdqfielvesylgrileIQENVVEPSGKGPCPNLLSAQVD-------LLEWMSDGSSKTK----------- 302
Cdd:PLN02789 227 FKDD----------------------KEALVSDPEVSSVCLEVLSKDSNhvfalsdLLDLLCEGLQPTAefrdtvdtlae 284
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 219118556 303 -------ALDYLEELKTHDPIRKRYWAMRQQQIQAL 331
Cdd:PLN02789 285 elsdstlAQAVCSELEVADPMRRNYWAWRKSKLPKA 320
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
12-328 7.06e-32

Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 121.52  E-value: 7.06e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  12 FADLAPIPQQ-DGPHAVCRIDYPPDFTLAYDYMRALWKADERSRRALDLTTLCLELNPANYTVWHFRRLCLEALNLRNDQ 90
Cdd:COG5536    6 LRRVKPLPIQfDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSED 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556  91 TQIGVD--LALAADLGGSNPKNYQIWYHRRALLEKLDNPKILRdychqELSYIASVIVKDGKNYHAWSHRQWILRTLNDD 168
Cdd:COG5536   86 KEHLLDneLDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGR-----ELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 169 TAWTD---EVLYTEYLIDEDLRNNSAWNGR--WFAVHRGQKELLSvETDGPAQADYAIKIARLDPYNESPWRFLIAVLNE 243
Cdd:COG5536  161 FNFSDlkhELEYTTSLIETDIYNNSAWHHRyiWIERRFNRGDVIS-QKYLEKELEYIFDKIFTDPDNQSVWGYLRGVSSE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219118556 244 qrPQLSHDQFIELVESYLGRILEIQENVVEPSGK---GPCPNLLSAQVDLLEW---MSDGSSKTKAldYLEELKTHDPIR 317
Cdd:COG5536  240 --FATDIVMIGEKVEDLGKYIVIINGKELDLGPKenlPCLHSLLELEFLCHAEkalLTERDIEQKA--LVELAIKVDPAR 315
                        330
                 ....*....|.
gi 219118556 318 KRYWAMRQQQI 328
Cdd:COG5536  316 RNLYSTLHERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
135-165 2.14e-05

Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognize a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognizes a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family.


Pssm-ID: 460128 [Multi-domain]  Cd Length: 32  Bit Score: 40.70  E-value: 2.14e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 219118556  135 HQELSYIASVIVKDGKNYHAWSHRQWILRTL 165
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
54-84 2.19e-04

Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognize a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognizes a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family.


Pssm-ID: 460128 [Multi-domain]  Cd Length: 32  Bit Score: 38.00  E-value: 2.19e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 219118556   54 RRALDLTTLCLELNPANYTVWHFRRLCLEAL 84
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
96-124 2.79e-03

Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and geranylgeranyltransferase 1 (GGT1) recognize a CaaX motif on their substrates where 'a' stands for preferably aliphatic residues, whereas GGT2 recognizes a completely different motif. Important substrates for FT include, amongst others, many members of the Ras superfamily. GGT1 substrates include some of the other small GTPases and GGT2 substrates include the Rab family.


Pssm-ID: 460128 [Multi-domain]  Cd Length: 32  Bit Score: 34.92  E-value: 2.79e-03
                          10        20
                  ....*....|....*....|....*....
gi 219118556   96 DLALAADLGGSNPKNYQIWYHRRALLEKL 124
Cdd:pfam01239   4 ELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
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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