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Conserved domains on  [gi|2080985497|ref|XP_042879193|]
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protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha-like [Penaeus japonicus]

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

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PLN02789 super family cl33568
farnesyltranstransferase
13-319 1.61e-110

farnesyltranstransferase


The actual alignment was detected with superfamily member PLN02789:

Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 324.01  E-value: 1.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  13 EAWVFYKDREEWADVTPVPQDDGPNPVVKIAYTDAFTDVYDYFRAVMASGELSERALELTEDALNMNAANYTVWQYRRKI 92
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  93 LKHLGNDLEDELNFCRHMIELNPKNYQVWHHRRVIVEWLGD--ASKELRLTEIIFSQDAKNYHAWEHRQWVLRTFKLFDG 170
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 171 ELDYVDRLLEEDARNNSAWNQRHFTITQTT---GFTPDViEREVKYAKKAISKVIGNESPWSYLRGVLQHCDSGLGSVCD 247
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPllgGLEAMR-DSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 248 LEQWCQQMYESGERSPHLLTFMLDLMEDKMERETSERESTLKKSLD---------MCEALAVeHDQIRREYWRYIARNLS 318
Cdd:PLN02789  240 VSSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTLAEElsdstlaqaVCSELEV-ADPMRRNYWAWRKSKLP 318

                  .
gi 2080985497 319 H 319
Cdd:PLN02789  319 K 319
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
13-319 1.61e-110

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 324.01  E-value: 1.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  13 EAWVFYKDREEWADVTPVPQDDGPNPVVKIAYTDAFTDVYDYFRAVMASGELSERALELTEDALNMNAANYTVWQYRRKI 92
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  93 LKHLGNDLEDELNFCRHMIELNPKNYQVWHHRRVIVEWLGD--ASKELRLTEIIFSQDAKNYHAWEHRQWVLRTFKLFDG 170
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 171 ELDYVDRLLEEDARNNSAWNQRHFTITQTT---GFTPDViEREVKYAKKAISKVIGNESPWSYLRGVLQHCDSGLGSVCD 247
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPllgGLEAMR-DSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 248 LEQWCQQMYESGERSPHLLTFMLDLMEDKMERETSERESTLKKSLD---------MCEALAVeHDQIRREYWRYIARNLS 318
Cdd:PLN02789  240 VSSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTLAEElsdstlaqaVCSELEV-ADPMRRNYWAWRKSKLP 318

                  .
gi 2080985497 319 H 319
Cdd:PLN02789  319 K 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
26-317 1.25e-44

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 155.03  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  26 DVTPVP-QDDGPNPVVKIAYTDAFTDVYDYFRAVMASGELSERALELTEDALNMNAANYTVWQYRRKILKHLGNDLED-- 102
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 103 -----ELNFCRHMIELNPKNYQVWHHRRVIVEWLGDAS--KELRLTEIIFSQDAKNYHAWEHRQWVLRT------FKLFD 169
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSwgRELFITKKLLDSDSRNYHVWSYRRWVLRTiedlfnFSDLK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 170 GELDYVDRLLEEDARNNSAWNQRH---FTITQTTGFTPDV-IEREVKYAKKAISKVIGNESPWSYLRGVLQHC----DSG 241
Cdd:COG5536   168 HELEYTTSLIETDIYNNSAWHHRYiwiERRFNRGDVISQKyLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFatdiVMI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 242 LGSVCDLEQWCQ--QMYESGERSPHLLTFM--LDLMEDKMERE---TSERESTLKKSLDmceaLAVEHDQIRREYWRYIA 314
Cdd:COG5536   248 GEKVEDLGKYIViiNGKELDLGPKENLPCLhsLLELEFLCHAEkalLTERDIEQKALVE----LAIKVDPARRNLYSTLH 323

                  ...
gi 2080985497 315 RNL 317
Cdd:COG5536   324 ERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
100-131 1.22e-07

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: 47.25  E-value: 1.22e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2080985497 100 LEDELNFCRHMIELNPKNYQVWHHRRVIVEWL 131
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
PLN02789 PLN02789
farnesyltranstransferase
13-319 1.61e-110

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 324.01  E-value: 1.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  13 EAWVFYKDREEWADVTPVPQDDGPNPVVKIAYTDAFTDVYDYFRAVMASGELSERALELTEDALNMNAANYTVWQYRRKI 92
Cdd:PLN02789    1 DEWVPLSQRPEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  93 LKHLGNDLEDELNFCRHMIELNPKNYQVWHHRRVIVEWLGD--ASKELRLTEIIFSQDAKNYHAWEHRQWVLRTFKLFDG 170
Cdd:PLN02789   81 LEALDADLEEELDFAEDVAEDNPKNYQIWHHRRWLAEKLGPdaANKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWED 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 171 ELDYVDRLLEEDARNNSAWNQRHFTITQTT---GFTPDViEREVKYAKKAISKVIGNESPWSYLRGVLQHCDSGLGSVCD 247
Cdd:PLN02789  161 ELEYCHQLLEEDVRNNSAWNQRYFVITRSPllgGLEAMR-DSELKYTIDAILANPRNESPWRYLRGLFKDDKEALVSDPE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 248 LEQWCQQMYESGERSPHLLTFMLDLMEDKMERETSERESTLKKSLD---------MCEALAVeHDQIRREYWRYIARNLS 318
Cdd:PLN02789  240 VSSVCLEVLSKDSNHVFALSDLLDLLCEGLQPTAEFRDTVDTLAEElsdstlaqaVCSELEV-ADPMRRNYWAWRKSKLP 318

                  .
gi 2080985497 319 H 319
Cdd:PLN02789  319 K 319
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
26-317 1.25e-44

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 155.03  E-value: 1.25e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  26 DVTPVP-QDDGPNPVVKIAYTDAFTDVYDYFRAVMASGELSERALELTEDALNMNAANYTVWQYRRKILKHLGNDLED-- 102
Cdd:COG5536     8 RVKPLPiQFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMVSEDke 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 103 -----ELNFCRHMIELNPKNYQVWHHRRVIVEWLGDAS--KELRLTEIIFSQDAKNYHAWEHRQWVLRT------FKLFD 169
Cdd:COG5536    88 hlldnELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSwgRELFITKKLLDSDSRNYHVWSYRRWVLRTiedlfnFSDLK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 170 GELDYVDRLLEEDARNNSAWNQRH---FTITQTTGFTPDV-IEREVKYAKKAISKVIGNESPWSYLRGVLQHC----DSG 241
Cdd:COG5536   168 HELEYTTSLIETDIYNNSAWHHRYiwiERRFNRGDVISQKyLEKELEYIFDKIFTDPDNQSVWGYLRGVSSEFatdiVMI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497 242 LGSVCDLEQWCQ--QMYESGERSPHLLTFM--LDLMEDKMERE---TSERESTLKKSLDmceaLAVEHDQIRREYWRYIA 314
Cdd:COG5536   248 GEKVEDLGKYIViiNGKELDLGPKENLPCLhsLLELEFLCHAEkalLTERDIEQKALVE----LAIKVDPARRNLYSTLH 323

                  ...
gi 2080985497 315 RNL 317
Cdd:COG5536   324 ERF 326
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
100-131 1.22e-07

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: 47.25  E-value: 1.22e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2080985497 100 LEDELNFCRHMIELNPKNYQVWHHRRVIVEWL 131
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
66-192 1.18e-06

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.85  E-value: 1.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  66 ERALELTEDALNMNAANYTVWQYRRKILKHLGnDLEDELNFCRHMIELNPKNYQVWHHRRVIVEWLGDASKELRLTEIIF 145
Cdd:COG0457    25 EEAIEDYEKALELDPDDAEALYNLGLAYLRLG-RYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKAL 103
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2080985497 146 SQDAKNYHAWEHRQWVLRTFKLFDGELDYVDRLLEEDARNNSAWNQR 192
Cdd:COG0457   104 ELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNL 150
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
66-184 2.30e-05

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 45.00  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  66 ERALELTEDALNMNAANYTVWQYRRKILKHLGnDLEDELNFCRHMIELNPKNYQVWHHRRVIVEWLGDASKELRLTEIIF 145
Cdd:COG0457    59 EEALADYEQALELDPDDAEALNNLGLALQALG-RYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERAL 137
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2080985497 146 SQDAKNYHAWEHRQWVLRTFKLFDGELDYVDRLLEEDAR 184
Cdd:COG0457   138 ELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALA 176
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
135-165 2.78e-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: 37.62  E-value: 2.78e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2080985497 135 SKELRLTEIIFSQDAKNYHAWEHRQWVLRTF 165
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
66-185 3.31e-04

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 40.18  E-value: 3.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2080985497  66 ERALELTEDALNMNAANYTVWQYRRKILKHLGnDLEDELNFCRHMIELNPKNYQVWHHRRVIVEWLGDASKELRLTEIIF 145
Cdd:COG4783    21 DEAEALLEKALELDPDNPEAFALLGEILLQLG-DLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKAL 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2080985497 146 SQDAKNYHAWEHRQWVLRTFKLFDGELDYVDRLLEEDARN 185
Cdd:COG4783   100 KLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELDPDD 139
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
66-96 3.56e-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: 37.23  E-value: 3.56e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2080985497  66 ERALELTEDALNMNAANYTVWQYRRKILKHL 96
Cdd:pfam01239   2 EEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
168-198 3.22e-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: 34.54  E-value: 3.22e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2080985497 168 FDGELDYVDRLLEEDARNNSAWNQRHFTITQ 198
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
 
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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