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Conserved domains on  [gi|119583593|gb|EAW63189|]
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farnesyltransferase, CAAX box, alpha, isoform CRA_b [Homo sapiens]

Protein Classification

protein prenyltransferase subunit alpha family protein( domain architecture ID 1002166)

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

CATH:  1.25.40.120
PubMed:  1918005
SCOP:  4001331

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02789 super family cl33568
farnesyltranstransferase
142-407 7.49e-85

farnesyltranstransferase


The actual alignment was detected with superfamily member PLN02789:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 261.99  E-value: 7.49e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 142 VLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTV---------- 211
Cdd:PLN02789   4 VPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVwhfrrlclea 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 212 --------------------------HHRRVLVEWLRD--PSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQ 263
Cdd:PLN02789  84 ldadleeeldfaedvaednpknyqiwHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 264 YVDQLLKEDVRNNSVWNQRYFVISNTTGYND-RAVLEREVQYTLEMIKLVPHNESAWNYLKGIL--QDRGLSKYPNLLNQ 340
Cdd:PLN02789 164 YCHQLLEEDVRNNSAWNQRYFVITRSPLLGGlEAMRDSELKYTIDAILANPRNESPWRYLRGLFkdDKEALVSDPEVSSV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119583593 341 -LLDLQPSHSSPYLIAFLVDIYED---MLENQCDNKEDI------LNKALELCEILAKEkDTIRKEYWRYIGRSLQS 407
Cdd:PLN02789 244 cLEVLSKDSNHVFALSDLLDLLCEglqPTAEFRDTVDTLaeelsdSTLAQAVCSELEVA-DPMRRNYWAWRKSKLPK 319
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
142-407 7.49e-85

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 261.99  E-value: 7.49e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 142 VLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTV---------- 211
Cdd:PLN02789   4 VPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVwhfrrlclea 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 212 --------------------------HHRRVLVEWLRD--PSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQ 263
Cdd:PLN02789  84 ldadleeeldfaedvaednpknyqiwHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 264 YVDQLLKEDVRNNSVWNQRYFVISNTTGYND-RAVLEREVQYTLEMIKLVPHNESAWNYLKGIL--QDRGLSKYPNLLNQ 340
Cdd:PLN02789 164 YCHQLLEEDVRNNSAWNQRYFVITRSPLLGGlEAMRDSELKYTIDAILANPRNESPWRYLRGLFkdDKEALVSDPEVSSV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119583593 341 -LLDLQPSHSSPYLIAFLVDIYED---MLENQCDNKEDI------LNKALELCEILAKEkDTIRKEYWRYIGRSLQS 407
Cdd:PLN02789 244 cLEVLSKDSNHVFALSDLLDLLCEglqPTAEFRDTVDTLaeelsdSTLAQAVCSELEVA-DPMRRNYWAWRKSKLPK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
158-326 2.08e-24

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 102.64  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 158 QNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTV-------------------------- 211
Cdd:COG5536   15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIwnyrfsilkhvqmvsedkehlldnel 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 212 -----------------HHRRVLVEWLRDPS--QELEFIADILNQDAKNYHAWQHRQWV------IQEFKLWDNELQYVD 266
Cdd:COG5536   95 dfldealkdnpknyqiwHHRQWMLELFPKPSwgRELFITKKLLDSDSRNYHVWSYRRWVlrtiedLFNFSDLKHELEYTT 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583593 267 QLLKEDVRNNSVWNQRY---FVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGIL 326
Cdd:COG5536  175 SLIETDIYNNSAWHHRYiwiERRFNRGDVISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVS 237
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
224-255 3.12e-06

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: 43.40  E-value: 3.12e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119583593  224 PSQELEFIADILNQDAKNYHAWQHRQWVIQEF 255
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
142-407 7.49e-85

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 261.99  E-value: 7.49e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 142 VLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTV---------- 211
Cdd:PLN02789   4 VPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVwhfrrlclea 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 212 --------------------------HHRRVLVEWLRD--PSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQ 263
Cdd:PLN02789  84 ldadleeeldfaedvaednpknyqiwHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 264 YVDQLLKEDVRNNSVWNQRYFVISNTTGYND-RAVLEREVQYTLEMIKLVPHNESAWNYLKGIL--QDRGLSKYPNLLNQ 340
Cdd:PLN02789 164 YCHQLLEEDVRNNSAWNQRYFVITRSPLLGGlEAMRDSELKYTIDAILANPRNESPWRYLRGLFkdDKEALVSDPEVSSV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119583593 341 -LLDLQPSHSSPYLIAFLVDIYED---MLENQCDNKEDI------LNKALELCEILAKEkDTIRKEYWRYIGRSLQS 407
Cdd:PLN02789 244 cLEVLSKDSNHVFALSDLLDLLCEglqPTAEFRDTVDTLaeelsdSTLAQAVCSELEVA-DPMRRNYWAWRKSKLPK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
158-326 2.08e-24

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 102.64  E-value: 2.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 158 QNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTV-------------------------- 211
Cdd:COG5536   15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIwnyrfsilkhvqmvsedkehlldnel 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119583593 212 -----------------HHRRVLVEWLRDPS--QELEFIADILNQDAKNYHAWQHRQWV------IQEFKLWDNELQYVD 266
Cdd:COG5536   95 dfldealkdnpknyqiwHHRQWMLELFPKPSwgRELFITKKLLDSDSRNYHVWSYRRWVlrtiedLFNFSDLKHELEYTT 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119583593 267 QLLKEDVRNNSVWNQRY---FVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGIL 326
Cdd:COG5536  175 SLIETDIYNNSAWHHRYiwiERRFNRGDVISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVS 237
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
224-255 3.12e-06

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: 43.40  E-value: 3.12e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119583593  224 PSQELEFIADILNQDAKNYHAWQHRQWVIQEF 255
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
258-288 2.51e-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: 2.51e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 119583593  258 WDNELQYVDQLLKEDVRNNSVWNQRYFVISN 288
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
298-327 6.57e-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: 36.85  E-value: 6.57e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 119583593  298 LEREVQYTLEMIKLVPHNESAWNYLKGILQ 327
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLE 30
 
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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