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Conserved domains on  [gi|34782840|gb|AAH17029|]
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FNTA protein, partial [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
61-362 1.34e-113

farnesyltranstransferase


The actual alignment was detected with superfamily member PLN02789:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 333.64  E-value: 1.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840   61 VLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKS 140
Cdd:PLN02789   4 VPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  141 LQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRD--PSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQ 218
Cdd:PLN02789  84 LDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  219 YVDQLLKEDVRNNSVWNQRYFVISNTTGYND-RAVLEREVQYTLEMIKLVPHNESAWNYLKGIL--QDRGLSKYPNLLNQ 295
Cdd:PLN02789 164 YCHQLLEEDVRNNSAWNQRYFVITRSPLLGGlEAMRDSELKYTIDAILANPRNESPWRYLRGLFkdDKEALVSDPEVSSV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34782840  296 -LLDLQPSHSSPYLIAFLVDIYED---MLENQCDNKEDI------LNKALELCEILAKEkDTIRKEYWRYIGRSLQS 362
Cdd:PLN02789 244 cLEVLSKDSNHVFALSDLLDLLCEglqPTAEFRDTVDTLaeelsdSTLAQAVCSELEVA-DPMRRNYWAWRKSKLPK 319
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
61-362 1.34e-113

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 333.64  E-value: 1.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840   61 VLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKS 140
Cdd:PLN02789   4 VPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  141 LQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRD--PSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQ 218
Cdd:PLN02789  84 LDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  219 YVDQLLKEDVRNNSVWNQRYFVISNTTGYND-RAVLEREVQYTLEMIKLVPHNESAWNYLKGIL--QDRGLSKYPNLLNQ 295
Cdd:PLN02789 164 YCHQLLEEDVRNNSAWNQRYFVITRSPLLGGlEAMRDSELKYTIDAILANPRNESPWRYLRGLFkdDKEALVSDPEVSSV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34782840  296 -LLDLQPSHSSPYLIAFLVDIYED---MLENQCDNKEDI------LNKALELCEILAKEkDTIRKEYWRYIGRSLQS 362
Cdd:PLN02789 244 cLEVLSKDSNHVFALSDLLDLLCEglqPTAEFRDTVDTLaeelsdSTLAQAVCSELEVA-DPMRRNYWAWRKSKLPK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
77-281 1.25e-38

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 140.78  E-value: 1.25e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  77 QNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHE-------EM 149
Cdd:COG5536  15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDkehlldnEL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840 150 NYITAIIEEQPKNYQVWHHRRVLVEWLRDPS--QELEFIADILNQDAKNYHAWQHRQWV------IQEFKLWDNELQYVD 221
Cdd:COG5536  95 DFLDEALKDNPKNYQIWHHRQWMLELFPKPSwgRELFITKKLLDSDSRNYHVWSYRRWVlrtiedLFNFSDLKHELEYTT 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34782840 222 QLLKEDVRNNSVWNQRY---FVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGIL 281
Cdd:COG5536 175 SLIETDIYNNSAWHHRYiwiERRFNRGDVISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVS 237
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
145-176 9.43e-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: 41.85  E-value: 9.43e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 34782840   145 LHEEMNYITAIIEEQPKNYQVWHHRRVLVEWL 176
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
61-362 1.34e-113

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 333.64  E-value: 1.34e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840   61 VLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKS 140
Cdd:PLN02789   4 VPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  141 LQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRD--PSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQ 218
Cdd:PLN02789  84 LDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  219 YVDQLLKEDVRNNSVWNQRYFVISNTTGYND-RAVLEREVQYTLEMIKLVPHNESAWNYLKGIL--QDRGLSKYPNLLNQ 295
Cdd:PLN02789 164 YCHQLLEEDVRNNSAWNQRYFVITRSPLLGGlEAMRDSELKYTIDAILANPRNESPWRYLRGLFkdDKEALVSDPEVSSV 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 34782840  296 -LLDLQPSHSSPYLIAFLVDIYED---MLENQCDNKEDI------LNKALELCEILAKEkDTIRKEYWRYIGRSLQS 362
Cdd:PLN02789 244 cLEVLSKDSNHVFALSDLLDLLCEglqPTAEFRDTVDTLaeelsdSTLAQAVCSELEVA-DPMRRNYWAWRKSKLPK 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
77-281 1.25e-38

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 140.78  E-value: 1.25e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840  77 QNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHE-------EM 149
Cdd:COG5536  15 QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDkehlldnEL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840 150 NYITAIIEEQPKNYQVWHHRRVLVEWLRDPS--QELEFIADILNQDAKNYHAWQHRQWV------IQEFKLWDNELQYVD 221
Cdd:COG5536  95 DFLDEALKDNPKNYQIWHHRQWMLELFPKPSwgRELFITKKLLDSDSRNYHVWSYRRWVlrtiedLFNFSDLKHELEYTT 174
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 34782840 222 QLLKEDVRNNSVWNQRY---FVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGIL 281
Cdd:COG5536 175 SLIETDIYNNSAWHHRYiwiERRFNRGDVISQKYLEKELEYIFDKIFTDPDNQSVWGYLRGVS 237
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
145-176 9.43e-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: 41.85  E-value: 9.43e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 34782840   145 LHEEMNYITAIIEEQPKNYQVWHHRRVLVEWL 176
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
179-210 1.56e-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: 41.47  E-value: 1.56e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 34782840   179 PSQELEFIADILNQDAKNYHAWQHRQWVIQEF 210
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
103-237 4.97e-04

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.15  E-value: 4.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840 103 VLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLqKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQE 182
Cdd:COG0457  17 AYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRL-GRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEA 95
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 34782840 183 LEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR 237
Cdd:COG0457  96 LEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
111-141 8.14e-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: 36.46  E-value: 8.14e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 34782840   111 ERAFKLTRDAIELNAANYTVWHFRRVLLKSL 141
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
213-243 1.00e-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: 36.08  E-value: 1.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 34782840   213 WDNELQYVDQLLKEDVRNNSVWNQRYFVISN 243
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
253-282 2.50e-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: 35.31  E-value: 2.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 34782840   253 LEREVQYTLEMIKLVPHNESAWNYLKGILQ 282
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLE 30
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
103-229 3.24e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.83  E-value: 3.24e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34782840 103 VLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLqKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQE 182
Cdd:COG0457  51 AYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQAL-GRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEA 129
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 34782840 183 LEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVR 229
Cdd:COG0457 130 IEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
 
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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