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Conserved domains on  [gi|194368682]
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Chain A, Geranylgeranyl transferase type-2 subunit alpha

Protein Classification

protein prenyltransferase subunit alpha family protein( domain architecture ID 1904589)

protein prenyltransferase subunit alpha family protein such as geranylgeranyl transferase type-2 subunit alpha, which catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to proteins having the C-terminal -XCC or -XCXC, where both cysteines may become modified

CATH:  1.25.40.120
EC:  2.5.1.-
Gene Ontology:  GO:0008318|GO:0018342
PubMed:  18756270|1622936
SCOP:  4001331

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BET4 super family cl44255
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
5-322 2.01e-56

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


The actual alignment was detected with superfamily member COG5536:

Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 186.23  E-value: 2.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682   5 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETE 83
Cdd:COG5536    3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682  84 KSPEESaaLVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVA 163
Cdd:COG5536   83 SEDKEH--LLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 164 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQgrlpeNVLLKELELVQNAFFTDPNDQSAWFYHRW 238
Cdd:COG5536  161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQ-----KYLEKELEYIFDKIFTDPDNQSVWGYLRG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 239 LLGAGSGRCELSVEKSTVLQSELE--SCKELQELEPENKWCLLTIIL---LMRALDPLLYEKETLQYFSTLKA--VDPMR 311
Cdd:COG5536  236 VSSEFATDIVMIGEKVEDLGKYIViiNGKELDLGPKENLPCLHSLLElefLCHAEKALLTERDIEQKALVELAikVDPAR 315
                        330
                 ....*....|.
gi 194368682 312 AAYLDDLRSKF 322
Cdd:COG5536  316 RNLYSTLHERF 326
 
Name Accession Description Interval E-value
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
5-322 2.01e-56

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 186.23  E-value: 2.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682   5 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETE 83
Cdd:COG5536    3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682  84 KSPEESaaLVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVA 163
Cdd:COG5536   83 SEDKEH--LLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 164 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQgrlpeNVLLKELELVQNAFFTDPNDQSAWFYHRW 238
Cdd:COG5536  161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQ-----KYLEKELEYIFDKIFTDPDNQSVWGYLRG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 239 LLGAGSGRCELSVEKSTVLQSELE--SCKELQELEPENKWCLLTIIL---LMRALDPLLYEKETLQYFSTLKA--VDPMR 311
Cdd:COG5536  236 VSSEFATDIVMIGEKVEDLGKYIViiNGKELDLGPKENLPCLHSLLElefLCHAEKALLTERDIEQKALVELAikVDPAR 315
                        330
                 ....*....|.
gi 194368682 312 AAYLDDLRSKF 322
Cdd:COG5536  316 RNLYSTLHERF 326
PLN02789 PLN02789
farnesyltranstransferase
44-314 1.33e-23

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 99.05  E-value: 1.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682  44 QAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETEkspeesaalVKAELGFLESCLRVNPKSYGTWHHRCWLLSR 123
Cdd:PLN02789  48 ASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDAD---------LEEELDFAEDVAEDNPKNYQIWHHRRWLAEK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 124 LPEPNWARELELCARFLEADERNFHCWDYRRFvAAQAAVAPAEELAFTDSLITRNFSNYSSWHYR------SCLLPQLHP 197
Cdd:PLN02789 119 LGPDAANKELEFTRKILSLDAKNYHAWSHRQW-VLRTLGGWEDELEYCHQLLEEDVRNNSAWNQRyfvitrSPLLGGLEA 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 198 QPDSgpqgrlpenvllkELELVQNAFFTDPNDQSAWFYHRWLLG----------AGSGRC--ELSVEKSTV--LQSELES 263
Cdd:PLN02789 198 MRDS-------------ELKYTIDAILANPRNESPWRYLRGLFKddkealvsdpEVSSVCleVLSKDSNHVfaLSDLLDL 264
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194368682 264 CKElqELEPENKWCLLTIILLMRALDPLLYeketLQYFSTLKAVDPMRAAY 314
Cdd:PLN02789 265 LCE--GLQPTAEFRDTVDTLAEELSDSTLA----QAVCSELEVADPMRRNY 309
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
166-195 6.99e-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: 39.54  E-value: 6.99e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 194368682  166 EELAFTDSLITRNFSNYSSWHYRSCLLPQL 195
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
5-322 2.01e-56

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 186.23  E-value: 2.01e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682   5 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETE 83
Cdd:COG5536    3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682  84 KSPEESaaLVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVA 163
Cdd:COG5536   83 SEDKEH--LLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 164 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQgrlpeNVLLKELELVQNAFFTDPNDQSAWFYHRW 238
Cdd:COG5536  161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQ-----KYLEKELEYIFDKIFTDPDNQSVWGYLRG 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 239 LLGAGSGRCELSVEKSTVLQSELE--SCKELQELEPENKWCLLTIIL---LMRALDPLLYEKETLQYFSTLKA--VDPMR 311
Cdd:COG5536  236 VSSEFATDIVMIGEKVEDLGKYIViiNGKELDLGPKENLPCLHSLLElefLCHAEKALLTERDIEQKALVELAikVDPAR 315
                        330
                 ....*....|.
gi 194368682 312 AAYLDDLRSKF 322
Cdd:COG5536  316 RNLYSTLHERF 326
PLN02789 PLN02789
farnesyltranstransferase
44-314 1.33e-23

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 99.05  E-value: 1.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682  44 QAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETEkspeesaalVKAELGFLESCLRVNPKSYGTWHHRCWLLSR 123
Cdd:PLN02789  48 ASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDAD---------LEEELDFAEDVAEDNPKNYQIWHHRRWLAEK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 124 LPEPNWARELELCARFLEADERNFHCWDYRRFvAAQAAVAPAEELAFTDSLITRNFSNYSSWHYR------SCLLPQLHP 197
Cdd:PLN02789 119 LGPDAANKELEFTRKILSLDAKNYHAWSHRQW-VLRTLGGWEDELEYCHQLLEEDVRNNSAWNQRyfvitrSPLLGGLEA 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 194368682 198 QPDSgpqgrlpenvllkELELVQNAFFTDPNDQSAWFYHRWLLG----------AGSGRC--ELSVEKSTV--LQSELES 263
Cdd:PLN02789 198 MRDS-------------ELKYTIDAILANPRNESPWRYLRGLFKddkealvsdpEVSSVCleVLSKDSNHVfaLSDLLDL 264
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 194368682 264 CKElqELEPENKWCLLTIILLMRALDPLLYeketLQYFSTLKAVDPMRAAY 314
Cdd:PLN02789 265 LCE--GLQPTAEFRDTVDTLAEELSDSTLA----QAVCSELEVADPMRRNY 309
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
166-195 6.99e-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: 39.54  E-value: 6.99e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 194368682  166 EELAFTDSLITRNFSNYSSWHYRSCLLPQL 195
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
93-124 2.88e-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: 2.88e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 194368682   93 VKAELGFLESCLRVNPKSYGTWHHRCWLLSRL 124
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
212-240 1.17e-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: 1.17e-03
                          10        20
                  ....*....|....*....|....*....
gi 194368682  212 LLKELELVQNAFFTDPNDQSAWFYHRWLL 240
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
 
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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