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Conserved domains on  [gi|19114430|ref|NP_593518|]
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geranylgeranyltransferase type 1 alpha subunit Cwp1 [Schizosaccharomyces pombe]

Protein Classification

protein prenyltransferase subunit alpha family protein( domain architecture ID 11475630)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
9-294 4.38e-116

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


:

Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 337.23  E-value: 4.38e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   9 NEILDFTEYGPLtPIpQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNH 88
Cdd:COG5536   1 PEDLDLRRVKPL-PI-QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430  89 -------TPSYIDNELEWLDEIAEDFQKNYQVWHHRQKILSL--TKNYERELEFTKKMFEIDSKNYHVWSYRVWIL---- 155
Cdd:COG5536  79 vqmvsedKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELfpKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtie 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 156 --QNFNDYSQELKLTNELLEKDIYNNSAWNHR---FYVLFETSKVVSWS-LEEELNYLKDKILFAPDNQSAWNYLCGVLD 229
Cdd:COG5536 159 dlFNFSDLKHELEYTTSLIETDIYNNSAWHHRyiwIERRFNRGDVISQKyLEKELEYIFDKIFTDPDNQSVWGYLRGVSS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 230 K------SGPSKLDNLIANL------------RKNLPALHKPL-LEFLAM-YEPSSSE-EIYQK----LANEVDVPHAAL 284
Cdd:COG5536 239 EfatdivMIGEKVEDLGKYIviingkeldlgpKENLPCLHSLLeLEFLCHaEKALLTErDIEQKalveLAIKVDPARRNL 318
                       330
                ....*....|
gi 19114430 285 WTWMSQRSNP 294
Cdd:COG5536 319 YSTLHERFNC 328
 
Name Accession Description Interval E-value
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
9-294 4.38e-116

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 337.23  E-value: 4.38e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   9 NEILDFTEYGPLtPIpQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNH 88
Cdd:COG5536   1 PEDLDLRRVKPL-PI-QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430  89 -------TPSYIDNELEWLDEIAEDFQKNYQVWHHRQKILSL--TKNYERELEFTKKMFEIDSKNYHVWSYRVWIL---- 155
Cdd:COG5536  79 vqmvsedKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELfpKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtie 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 156 --QNFNDYSQELKLTNELLEKDIYNNSAWNHR---FYVLFETSKVVSWS-LEEELNYLKDKILFAPDNQSAWNYLCGVLD 229
Cdd:COG5536 159 dlFNFSDLKHELEYTTSLIETDIYNNSAWHHRyiwIERRFNRGDVISQKyLEKELEYIFDKIFTDPDNQSVWGYLRGVSS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 230 K------SGPSKLDNLIANL------------RKNLPALHKPL-LEFLAM-YEPSSSE-EIYQK----LANEVDVPHAAL 284
Cdd:COG5536 239 EfatdivMIGEKVEDLGKYIviingkeldlgpKENLPCLHSLLeLEFLCHaEKALLTErDIEQKalveLAIKVDPARRNL 318
                       330
                ....*....|
gi 19114430 285 WTWMSQRSNP 294
Cdd:COG5536 319 YSTLHERFNC 328
PLN02789 PLN02789
farnesyltranstransferase
15-283 3.34e-72

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 225.01  E-value: 3.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   15 TEYGPLTPIPQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNHTPSYID 94
Cdd:PLN02789  10 PEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDADLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   95 NELEWLDEIAEDFQKNYQVWHHRQKIL-SLTKNY-ERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELL 172
Cdd:PLN02789  90 EELDFAEDVAEDNPKNYQIWHHRRWLAeKLGPDAaNKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELEYCHQLL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430  173 EKDIYNNSAWNHRFYVLFETSKV--VSWSLEEELNYLKDKILFAPDNQSAWNYLCGVL---------DKSGPSKLDNLIA 241
Cdd:PLN02789 170 EEDVRNNSAWNQRYFVITRSPLLggLEAMRDSELKYTIDAILANPRNESPWRYLRGLFkddkealvsDPEVSSVCLEVLS 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 19114430  242 NLRKNLPALHKPLLEFLAMYEPSSS-EEIYQKLANEVDVPHAA 283
Cdd:PLN02789 250 KDSNHVFALSDLLDLLCEGLQPTAEfRDTVDTLAEELSDSTLA 292
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
127-158 2.90e-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: 43.01  E-value: 2.90e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19114430   127 YERELEFTKKMFEIDSKNYHVWSYRVWILQNF 158
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
9-294 4.38e-116

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 337.23  E-value: 4.38e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   9 NEILDFTEYGPLtPIpQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNH 88
Cdd:COG5536   1 PEDLDLRRVKPL-PI-QFDLLSELQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKH 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430  89 -------TPSYIDNELEWLDEIAEDFQKNYQVWHHRQKILSL--TKNYERELEFTKKMFEIDSKNYHVWSYRVWIL---- 155
Cdd:COG5536  79 vqmvsedKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELfpKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLrtie 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 156 --QNFNDYSQELKLTNELLEKDIYNNSAWNHR---FYVLFETSKVVSWS-LEEELNYLKDKILFAPDNQSAWNYLCGVLD 229
Cdd:COG5536 159 dlFNFSDLKHELEYTTSLIETDIYNNSAWHHRyiwIERRFNRGDVISQKyLEKELEYIFDKIFTDPDNQSVWGYLRGVSS 238
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 230 K------SGPSKLDNLIANL------------RKNLPALHKPL-LEFLAM-YEPSSSE-EIYQK----LANEVDVPHAAL 284
Cdd:COG5536 239 EfatdivMIGEKVEDLGKYIviingkeldlgpKENLPCLHSLLeLEFLCHaEKALLTErDIEQKalveLAIKVDPARRNL 318
                       330
                ....*....|
gi 19114430 285 WTWMSQRSNP 294
Cdd:COG5536 319 YSTLHERFNC 328
PLN02789 PLN02789
farnesyltranstransferase
15-283 3.34e-72

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 225.01  E-value: 3.34e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   15 TEYGPLTPIPQDDGENPLAKICYTTGYEQGMAYFRAIMAKKEYSLRALNLTGFLIMNNPAHYTVWAYRFQILNHTPSYID 94
Cdd:PLN02789  10 PEWADVTPIPQDDGPNPVVPIAYTPEFREAMDYFRAVYASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDADLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430   95 NELEWLDEIAEDFQKNYQVWHHRQKIL-SLTKNY-ERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELL 172
Cdd:PLN02789  90 EELDFAEDVAEDNPKNYQIWHHRRWLAeKLGPDAaNKELEFTRKILSLDAKNYHAWSHRQWVLRTLGGWEDELEYCHQLL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430  173 EKDIYNNSAWNHRFYVLFETSKV--VSWSLEEELNYLKDKILFAPDNQSAWNYLCGVL---------DKSGPSKLDNLIA 241
Cdd:PLN02789 170 EEDVRNNSAWNQRYFVITRSPLLggLEAMRDSELKYTIDAILANPRNESPWRYLRGLFkddkealvsDPEVSSVCLEVLS 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 19114430  242 NLRKNLPALHKPLLEFLAMYEPSSS-EEIYQKLANEVDVPHAA 283
Cdd:PLN02789 250 KDSNHVFALSDLLDLLCEGLQPTAEfRDTVDTLAEELSDSTLA 292
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
127-158 2.90e-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: 43.01  E-value: 2.90e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19114430   127 YERELEFTKKMFEIDSKNYHVWSYRVWILQNF 158
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
97-256 1.34e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.30  E-value: 1.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430  97 LEWLDEIAEDFQKNYQVWHHRQKILSLTKNYERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELLEKDI 176
Cdd:COG0457  28 IEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDP 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 177 YNNSAWNHRFYVLFETSKvvswsLEEELNYLKDKILFAPDNQSAWNYLCGVLDKSGpsKLDNLIANLRKNLPALHKPLLE 256
Cdd:COG0457 108 DDAEALYNLGLALLELGR-----YDEAIEAYERALELDPDDADALYNLGIALEKLG--RYEEALELLEKLEAAALAALLA 180
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
161-189 2.94e-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: 2.94e-04
                          10        20
                  ....*....|....*....|....*....
gi 19114430   161 YSQELKLTNELLEKDIYNNSAWNHRFYVL 189
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLL 29
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
93-122 8.58e-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: 36.08  E-value: 8.58e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 19114430    93 IDNELEWLDEIAEDFQKNYQVWHHRQKILS 122
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLE 30
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
110-294 1.60e-03

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.98  E-value: 1.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 110 NYQVWHHRQKILSLTKNYERELEFTKKMFEIDSKNYHVWSYRVWILQNFNDYSQELKLTNELLEKDIYNNSAWNHRFYVL 189
Cdd:COG3914 111 NAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNAL 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19114430 190 FETSKvvswsLEEELNYLKDKILFAPDNQSAWNYLCGVLDKSGPSKLDNLIANLRKNLPALHKPLLEFLAMYEPSSSEE- 268
Cdd:COG3914 191 QDLGR-----LEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEELLAALARGPSELSPFALLYLPDDDPAe 265
                       170       180
                ....*....|....*....|....*....
gi 19114430 269 ---IYQKLANEVDVPHAALWTWMSQRSNP 294
Cdd:COG3914 266 llaLARAWAQLVAAAAAPELPPPPNPRDP 294
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
200-230 7.12e-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: 33.38  E-value: 7.12e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 19114430   200 LEEELNYLKDKILFAPDNQSAWNYLCGVLDK 230
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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