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Conserved domains on  [gi|31615536|pdb|1LTX|A]
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Chain A, RAB GERANYLGERANYLTRANSFERASE ALPHA SUBUNIT

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RabGGT_insert pfam07711
Rab geranylgeranyl transferase alpha-subunit, insert domain; Rab geranylgeranyl transferase ...
 247-346 3.72e-52

Rab geranylgeranyl transferase alpha-subunit, insert domain; Rab geranylgeranyl transferase (RabGGT) catalyzes the addition of two geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins, which is crucial for membrane association and function of these proteins in intracellular vesicular trafficking. This domain is inserted between pfam01239 repeats. This domain adopts an Ig-like fold and is thought to be involved in protein-protein interactions and might be involved in the recognition and binding of REP.


:

Pssm-ID: 462239  Cd Length: 101  Bit Score: 173.38  E-value: 3.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        247 CVHVSREEACLSVCFSRPLTVGSrmGTLLLMVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTGSD 326
Cdd:pfam07711   4 CLYVSREEERLAVAFSRPVNVGS--VTLMLVVDGSPLPVEWRTPRGRNRPSPVWLCDLPAGSLNDQRPQHTFTVHWTEGQ 81

                          90       100
                  ....*....|....*....|
1LTX_A        327 SQKECVLLKDRPECWCRDSA 346
Cdd:pfam07711  82 TQRECVLYKGRPESWCRDSA 101
BET4 super family cl44255
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 1-237 1.72e-49

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: 173.90  E-value: 1.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        1 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETE 79
Cdd:COG5536   3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A       80 KSPEESaaLVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVA 159
Cdd:COG5536  83 SEDKEH--LLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      160 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQgrlpeNVLLKELELVQNAFFTDPNDQSAWFYHRW 234
Cdd:COG5536 161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQ-----KYLEKELEYIFDKIFTDPDNQSVWGYLRG 235


                ...
1LTX_A      235 LLG 237
Cdd:COG5536 236 VSS 238
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 444-547 1.00e-11

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 64.81  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      444 RVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRA------LPPALAAL-RCLEVLQASDNALENVDGVANLPRLQELLLC 516
Cdd:cd21340  71 KKLYLGGNRISVVEGLENLTNLEELHIENQRLPPgekltfDPRSLAALsNSLRVLNISGNNIDSLEPLAPLRNLEQLDAS 150

                        90       100       110
                ....*....|....*....|....*....|..
1LTX_A      517 NNRLQQSAAIQPLVS-CPRLVLLNLQGNSLCQ 547
Cdd:cd21340 151 NNQISDLEELLDLLSsWPSLRELDLTGNPVCK 182
 
Name Accession Description Interval E-value
RabGGT_insert pfam07711
Rab geranylgeranyl transferase alpha-subunit, insert domain; Rab geranylgeranyl transferase ...
 247-346 3.72e-52

Rab geranylgeranyl transferase alpha-subunit, insert domain; Rab geranylgeranyl transferase (RabGGT) catalyzes the addition of two geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins, which is crucial for membrane association and function of these proteins in intracellular vesicular trafficking. This domain is inserted between pfam01239 repeats. This domain adopts an Ig-like fold and is thought to be involved in protein-protein interactions and might be involved in the recognition and binding of REP.


Pssm-ID: 462239  Cd Length: 101  Bit Score: 173.38  E-value: 3.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        247 CVHVSREEACLSVCFSRPLTVGSrmGTLLLMVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTGSD 326
Cdd:pfam07711   4 CLYVSREEERLAVAFSRPVNVGS--VTLMLVVDGSPLPVEWRTPRGRNRPSPVWLCDLPAGSLNDQRPQHTFTVHWTEGQ 81

                          90       100
                  ....*....|....*....|
1LTX_A        327 SQKECVLLKDRPECWCRDSA 346
Cdd:pfam07711  82 TQRECVLYKGRPESWCRDSA 101
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 1-237 1.72e-49

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 173.90  E-value: 1.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        1 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETE 79
Cdd:COG5536   3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A       80 KSPEESaaLVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVA 159
Cdd:COG5536  83 SEDKEH--LLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      160 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQgrlpeNVLLKELELVQNAFFTDPNDQSAWFYHRW 234
Cdd:COG5536 161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQ-----KYLEKELEYIFDKIFTDPDNQSVWGYLRG 235


                ...
1LTX_A      235 LLG 237
Cdd:COG5536 236 VSS 238
PLN02789 PLN02789
farnesyltranstransferase
 40-236 1.77e-20

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 92.50  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        40 QAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETEkspeesaalVKAELGFLESCLRVNPKSYGTWHHRCWLLSR 119
Cdd:PLN02789  48 ASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDAD---------LEEELDFAEDVAEDNPKNYQIWHHRRWLAEK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A       120 LPEPNWARELELCARFLEADERNFHCWDYRRFvAAQAAVAPAEELAFTDSLITRNFSNYSSWHYR------SCLLPQLHP 193
Cdd:PLN02789 119 LGPDAANKELEFTRKILSLDAKNYHAWSHRQW-VLRTLGGWEDELEYCHQLLEEDVRNNSAWNQRyfvitrSPLLGGLEA 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
1LTX_A       194 QPDSgpqgrlpenvllkELELVQNAFFTDPNDQSAWFYHRWLL 236
Cdd:PLN02789 198 MRDS-------------ELKYTIDAILANPRNESPWRYLRGLF 227
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 444-547 1.00e-11

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 64.81  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      444 RVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRA------LPPALAAL-RCLEVLQASDNALENVDGVANLPRLQELLLC 516
Cdd:cd21340  71 KKLYLGGNRISVVEGLENLTNLEELHIENQRLPPgekltfDPRSLAALsNSLRVLNISGNNIDSLEPLAPLRNLEQLDAS 150

                        90       100       110
                ....*....|....*....|....*....|..
1LTX_A      517 NNRLQQSAAIQPLVS-CPRLVLLNLQGNSLCQ 547
Cdd:cd21340 151 NNQISDLEELLDLLSsWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
444-545 5.66e-11

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.57  E-value: 5.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      444 RVLHLAHKDLTVL-CHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNALENVDGVANLPRLQELLLCNNRLQQ 522
Cdd:COG4886 185 KELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTD 264

                        90       100
                ....*....|....*....|...
1LTX_A      523 saaIQPLVSCPRLVLLNLQGNSL 545
Cdd:COG4886 265 ---LPPLANLTNLKTLDLSNNQL 284
LRR_9 pfam14580
Leucine-rich repeat;
468-562 4.69e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.37  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        468 LDLSHNRLRALPpALAALRCLEVLQASDNAL----ENVDGVanLPRLQELLLCNNRLQQSAAIQPLVSCPRLVLLNLQGN 543
Cdd:pfam14580  47 IDFSDNEIRKLD-GFPLLRRLKTLLLNNNRIcrigEGLGEA--LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRN 123

                          90
                  ....*....|....*....
1LTX_A        544 SLCQEEGIQERLAEMLPSV 562
Cdd:pfam14580 124 PVTNKPHYRLYVIYKVPQL 142
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-191 6.92e-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: 39.93  E-value: 6.92e-05
                          10        20        30
                  ....*....|....*....|....*....|
1LTX_A        162 EELAFTDSLITRNFSNYSSWHYRSCLLPQL 191
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
 
Name Accession Description Interval E-value
RabGGT_insert pfam07711
Rab geranylgeranyl transferase alpha-subunit, insert domain; Rab geranylgeranyl transferase ...
 247-346 3.72e-52

Rab geranylgeranyl transferase alpha-subunit, insert domain; Rab geranylgeranyl transferase (RabGGT) catalyzes the addition of two geranylgeranyl groups to the C-terminal cysteine residues of Rab proteins, which is crucial for membrane association and function of these proteins in intracellular vesicular trafficking. This domain is inserted between pfam01239 repeats. This domain adopts an Ig-like fold and is thought to be involved in protein-protein interactions and might be involved in the recognition and binding of REP.


Pssm-ID: 462239  Cd Length: 101  Bit Score: 173.38  E-value: 3.72e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        247 CVHVSREEACLSVCFSRPLTVGSrmGTLLLMVDEAPLSVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWTGSD 326
Cdd:pfam07711   4 CLYVSREEERLAVAFSRPVNVGS--VTLMLVVDGSPLPVEWRTPRGRNRPSPVWLCDLPAGSLNDQRPQHTFTVHWTEGQ 81

                          90       100
                  ....*....|....*....|
1LTX_A        327 SQKECVLLKDRPECWCRDSA 346
Cdd:pfam07711  82 TQRECVLYKGRPESWCRDSA 101
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 1-237 1.72e-49

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 173.90  E-value: 1.72e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        1 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETE 79
Cdd:COG5536   3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSILKHVQMV 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A       80 KSPEESaaLVKAELGFLESCLRVNPKSYGTWHHRCWLLSRLPEPNWARELELCARFLEADERNFHCWDYRRFVAAQAAVA 159
Cdd:COG5536  83 SEDKEH--LLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      160 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQgrlpeNVLLKELELVQNAFFTDPNDQSAWFYHRW 234
Cdd:COG5536 161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQ-----KYLEKELEYIFDKIFTDPDNQSVWGYLRG 235


                ...
1LTX_A      235 LLG 237
Cdd:COG5536 236 VSS 238
PLN02789 PLN02789
farnesyltranstransferase
 40-236 1.77e-20

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 92.50  E-value: 1.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        40 QAGELDESVLELTSQILGANPDFATLWNCRREVLQHLETEkspeesaalVKAELGFLESCLRVNPKSYGTWHHRCWLLSR 119
Cdd:PLN02789  48 ASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDAD---------LEEELDFAEDVAEDNPKNYQIWHHRRWLAEK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A       120 LPEPNWARELELCARFLEADERNFHCWDYRRFvAAQAAVAPAEELAFTDSLITRNFSNYSSWHYR------SCLLPQLHP 193
Cdd:PLN02789 119 LGPDAANKELEFTRKILSLDAKNYHAWSHRQW-VLRTLGGWEDELEYCHQLLEEDVRNNSAWNQRyfvitrSPLLGGLEA 197

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
1LTX_A       194 QPDSgpqgrlpenvllkELELVQNAFFTDPNDQSAWFYHRWLL 236
Cdd:PLN02789 198 MRDS-------------ELKYTIDAILANPRNESPWRYLRGLF 227
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 444-547 1.00e-11

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 64.81  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      444 RVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRA------LPPALAAL-RCLEVLQASDNALENVDGVANLPRLQELLLC 516
Cdd:cd21340  71 KKLYLGGNRISVVEGLENLTNLEELHIENQRLPPgekltfDPRSLAALsNSLRVLNISGNNIDSLEPLAPLRNLEQLDAS 150

                        90       100       110
                ....*....|....*....|....*....|..
1LTX_A      517 NNRLQQSAAIQPLVS-CPRLVLLNLQGNSLCQ 547
Cdd:cd21340 151 NNQISDLEELLDLLSsWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
444-545 5.66e-11

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 64.57  E-value: 5.66e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      444 RVLHLAHKDLTVL-CHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNALENVDGVANLPRLQELLLCNNRLQQ 522
Cdd:COG4886 185 KELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTD 264

                        90       100
                ....*....|....*....|...
1LTX_A      523 saaIQPLVSCPRLVLLNLQGNSL 545
Cdd:COG4886 265 ---LPPLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
351-545 9.81e-10

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.72  E-value: 9.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      351 LFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFSTLKAVDPMRAAYLDDLRSKFL 430
Cdd:COG4886   2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      431 LENSVLKMEYADvRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNALENV-DGVANLPR 509
Cdd:COG4886  82 LSLLLLGLTDLG-DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTN 160

                       170       180       190
                ....*....|....*....|....*....|....*..
1LTX_A      510 LQELLLCNNRLQQ-SAAIQPLvscPRLVLLNLQGNSL 545
Cdd:COG4886 161 LKSLDLSNNQLTDlPEELGNL---TNLKELDLSNNQI 194
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
444-545 1.46e-09

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 60.33  E-value: 1.46e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      444 RVLHLAHKDLTVL-CHLEQLLLVTHLDLSHNRLRALPPALAALRCLEVLQASDNALENV-DGVANLPRLQELLLCNNRLQ 521
Cdd:COG4886 162 KSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLT 241

                        90       100
                ....*....|....*....|....
1LTX_A      522 QsaaIQPLVSCPRLVLLNLQGNSL 545
Cdd:COG4886 242 D---LPELGNLTNLEELDLSNNQL 262
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 443-545 1.67e-09

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 58.26  E-value: 1.67e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      443 VRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRALPPaLAALRCLEVLQASDNALENVDGVANLPRLQELLLCNNRLQQ 522
Cdd:cd21340  26 LKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPP 104

                        90       100       110
                ....*....|....*....|....*....|.
1LTX_A      523 SaaiQPLVSCPR--------LVLLNLQGNSL 545
Cdd:cd21340 105 G---EKLTFDPRslaalsnsLRVLNISGNNI 132
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 465-550 3.29e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 51.33  E-value: 3.29e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      465 VTHLDLSHNRLRALPpALAALRCLEVLQASDNALENVDGVANLPRLQELLLCNNRLQQsaaIQPLVSCPRLVLLNLQGNS 544
Cdd:cd21340   4 ITHLYLNDKNITKID-NLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEK---IENLENLVNLKKLYLGGNR 79


                ....*.
1LTX_A      545 LCQEEG 550
Cdd:cd21340  80 ISVVEG 85
LRR_9 pfam14580
Leucine-rich repeat;
468-562 4.69e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 44.37  E-value: 4.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A        468 LDLSHNRLRALPpALAALRCLEVLQASDNAL----ENVDGVanLPRLQELLLCNNRLQQSAAIQPLVSCPRLVLLNLQGN 543
Cdd:pfam14580  47 IDFSDNEIRKLD-GFPLLRRLKTLLLNNNRIcrigEGLGEA--LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRN 123

                          90
                  ....*....|....*....
1LTX_A        544 SLCQEEGIQERLAEMLPSV 562
Cdd:pfam14580 124 PVTNKPHYRLYVIYKVPQL 142
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-191 6.92e-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: 39.93  E-value: 6.92e-05
                          10        20        30
                  ....*....|....*....|....*....|
1LTX_A        162 EELAFTDSLITRNFSNYSSWHYRSCLLPQL 191
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 89-120 2.82e-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: 38.39  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|..
1LTX_A         89 VKAELGFLESCLRVNPKSYGTWHHRCWLLSRL 120
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 208-238 9.82e-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: 9.82e-04
                          10        20        30
                  ....*....|....*....|....*....|.
1LTX_A        208 LLKELELVQNAFFTDPNDQSAWFYHRWLLGR 238
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
LRR_8 pfam13855
Leucine rich repeat;
443-498 3.42e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 3.42e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
1LTX_A        443 VRVLHLAHKDLTVLC--HLEQLLLVTHLDLSHNRLRALPP-ALAALRCLEVLQASDNAL 498
Cdd:pfam13855   3 LRSLDLSNNRLTSLDdgAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 351-548 5.87e-03

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 38.88  E-value: 5.87e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      351 LFRCELSVEKSTVLQSELEScKELQELEPENkwCLLTII---LLMRALDPLLYEKETLQYFSTLKAVDPMRAAyLDDLRS 427
Cdd:cd00116  88 LSDNALGPDGCGVLESLLRS-SSLQELKLNN--NGLGDRglrLLAKGLKDLPPALEKLVLGRNRLEGASCEAL-AKALRA 163

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1LTX_A      428 KFLLEnsVLKMEYADVRVLHLAH--KDLTVLCHLEqlllvtHLDLSHNRLR-----ALPPALAALRCLEVLQASDNALEN 500
Cdd:cd00116 164 NRDLK--ELNLANNGIGDAGIRAlaEGLKANCNLE------VLDLNNNGLTdegasALAETLASLKSLEVLNLGDNNLTD 235

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
1LTX_A      501 VdGVANL--------PRLQELLLCNNRLQQSAAI---QPLVSCPRLVLLNLQGNSLCQE 548
Cdd:cd00116 236 A-GAAALasallspnISLLTLSLSCNDITDDGAKdlaEVLAEKESLLELDLRGNKFGEE 293
 
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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