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Conserved domains on  [gi|53828918|ref|NP_004572|]
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geranylgeranyl transferase type-2 subunit alpha [Homo sapiens]

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 ...
 244-346 7.88e-54

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: 177.62  E-value: 7.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   244 ALRCLHVSRDEACLTVSFSRPLLVGSrmEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWT 323
Cdd:pfam07711   1 SIRCLYVSREEERLAVAFSRPVNVGS--VTLMLVVDGSPLPVEWRTPRGRNRPSPVWLCDLPAGSLNDQRPQHTFTVHWT 78

                          90       100
                  ....*....|....*....|...
gi 53828918   324 AGDVQKECVLLKGRQEGWCRDST 346
Cdd:pfam07711  79 EGQTQRECVLYKGRPESWCRDSA 101
BET4 super family cl44255
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 1-237 4.89e-48

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: 170.05  E-value: 4.89e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   1 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLqqLETQ 79
Cdd:COG5536   3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSIL--KHVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918  80 KSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVP 159
Cdd:COG5536  81 MVSEDKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 160 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPedvllKELELVQNAFFTDPNDQSAWFYHRW 234
Cdd:COG5536 161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQKYLE-----KELEYIFDKIFTDPDNQSVWGYLRG 235


                ...
gi 53828918 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 8.64e-14

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: 70.59  E-value: 8.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 444 RVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLR---TL---PPALAAL-RCLEVLQASDNAIESLDGVTNLPRLQELLLC 516
Cdd:cd21340  71 KKLYLGGNRISVVEGLENLTNLEELHIENQRLPpgeKLtfdPRSLAALsNSLRVLNISGNNIDSLEPLAPLRNLEQLDAS 150

                        90       100       110
                ....*....|....*....|....*....|..
gi 53828918 517 NNRLQQ-PAVLQPLASCPRLVLLNLQGNPLCQ 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 ...
 244-346 7.88e-54

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: 177.62  E-value: 7.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   244 ALRCLHVSRDEACLTVSFSRPLLVGSrmEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWT 323
Cdd:pfam07711   1 SIRCLYVSREEERLAVAFSRPVNVGS--VTLMLVVDGSPLPVEWRTPRGRNRPSPVWLCDLPAGSLNDQRPQHTFTVHWT 78

                          90       100
                  ....*....|....*....|...
gi 53828918   324 AGDVQKECVLLKGRQEGWCRDST 346
Cdd:pfam07711  79 EGQTQRECVLYKGRPESWCRDSA 101
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 1-237 4.89e-48

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 170.05  E-value: 4.89e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   1 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLqqLETQ 79
Cdd:COG5536   3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSIL--KHVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918  80 KSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVP 159
Cdd:COG5536  81 MVSEDKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 160 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPedvllKELELVQNAFFTDPNDQSAWFYHRW 234
Cdd:COG5536 161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQKYLE-----KELEYIFDKIFTDPDNQSVWGYLRG 235


                ...
gi 53828918 235 LLG 237
Cdd:COG5536 236 VSS 238
PLN02789 PLN02789
farnesyltranstransferase
 40-250 1.17e-22

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 99.05  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   40 QAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQkspeelaalVKAELGFLESCLRVNPKSYGTWHHRCWLLGR 119
Cdd:PLN02789  48 ASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDAD---------LEEELDFAEDVAEDNPKNYQIWHHRRWLAEK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918  120 LPEPNWTRELELCARFLEVDERNFHCWDYRRFVaTQAAVPPAEELAFTDSLITRNFSNYSSWHYR------SCLLPQLHP 193
Cdd:PLN02789 119 LGPDAANKELEFTRKILSLDAKNYHAWSHRQWV-LRTLGGWEDELEYCHQLLEEDVRNNSAWNQRyfvitrSPLLGGLEA 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53828918  194 QPDSgpqgrlpedvllkELELVQNAFFTDPNDQSAWFYHRWLLGR------ADPQDALRCLHV 250
Cdd:PLN02789 198 MRDS-------------ELKYTIDAILANPRNESPWRYLRGLFKDdkealvSDPEVSSVCLEV 247
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 444-547 8.64e-14

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: 70.59  E-value: 8.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 444 RVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLR---TL---PPALAAL-RCLEVLQASDNAIESLDGVTNLPRLQELLLC 516
Cdd:cd21340  71 KKLYLGGNRISVVEGLENLTNLEELHIENQRLPpgeKLtfdPRSLAALsNSLRVLNISGNNIDSLEPLAPLRNLEQLDAS 150

                        90       100       110
                ....*....|....*....|....*....|..
gi 53828918 517 NNRLQQ-PAVLQPLASCPRLVLLNLQGNPLCQ 547
Cdd:cd21340 151 NNQISDlEELLDLLSSWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
444-545 3.86e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 3.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 444 RVLHLAHKDLTVL-CHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLQQ 522
Cdd:COG4886 185 KELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTD 264

                        90       100
                ....*....|....*....|...
gi 53828918 523 pavLQPLASCPRLVLLNLQGNPL 545
Cdd:COG4886 265 ---LPPLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
351-558 2.81e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.73  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 351 LFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFQTLKAVDPMRATYLDDLRSKFL 430
Cdd:COG4886   2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 431 LENSVLKMEYAEvRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESL-DGVTNLPR 509
Cdd:COG4886  82 LSLLLLGLTDLG-DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 53828918 510 LQELLLCNNRLQQ-PAvlqPLASCPRLVLLNLQGNPLCQAVGILEQLAEL 558
Cdd:COG4886 161 LKSLDLSNNQLTDlPE---ELGNLTNLKELDLSNNQITDLPEPLGNLTNL 207
LRR_9 pfam14580
Leucine-rich repeat;
468-545 1.03e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 46.30  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   468 LDLSHNRLRTLPpALAALRCLEVLQASDNAI----ESLDGVtnLPRLQELLLCNNRLQQPAVLQPLASCPRLVLLNLQGN 543
Cdd:pfam14580  47 IDFSDNEIRKLD-GFPLLRRLKTLLLNNNRIcrigEGLGEA--LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRN 123


                  ..
gi 53828918   544 PL 545
Cdd:pfam14580 124 PV 125
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-191 4.11e-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: 40.70  E-value: 4.11e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 53828918   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 ...
 244-346 7.88e-54

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: 177.62  E-value: 7.88e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   244 ALRCLHVSRDEACLTVSFSRPLLVGSrmEILLLMVDDSPLIVEWRTPDGRNRPSHVWLCDLPAASLNDQLPQHTFRVIWT 323
Cdd:pfam07711   1 SIRCLYVSREEERLAVAFSRPVNVGS--VTLMLVVDGSPLPVEWRTPRGRNRPSPVWLCDLPAGSLNDQRPQHTFTVHWT 78

                          90       100
                  ....*....|....*....|...
gi 53828918   324 AGDVQKECVLLKGRQEGWCRDST 346
Cdd:pfam07711  79 EGQTQRECVLYKGRPESWCRDSA 101
BET4 COG5536
Protein prenyltransferase, alpha subunit [Posttranslational modification, protein turnover, ...
 1-237 4.89e-48

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


Pssm-ID: 227823 [Multi-domain]  Cd Length: 328  Bit Score: 170.05  E-value: 4.89e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   1 MHGRLKVKTSEEQAEAKR-LEREQKLKLYQSATQAVFQKRQAGELDESVLELTSQILGANPDFATLWNCRREVLqqLETQ 79
Cdd:COG5536   3 DLDLRRVKPLPIQFDLLSeLQRILYTESYHPLMGRFRAKRRKKEYSVRALKLTQELIDKNPEFYTIWNYRFSIL--KHVQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918  80 KSPEELAALVKAELGFLESCLRVNPKSYGTWHHRCWLLGRLPEPNWTRELELCARFLEVDERNFHCWDYRRFVATQAAVP 159
Cdd:COG5536  81 MVSEDKEHLLDNELDFLDEALKDNPKNYQIWHHRQWMLELFPKPSWGRELFITKKLLDSDSRNYHVWSYRRWVLRTIEDL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 160 P-----AEELAFTDSLITRNFSNYSSWHYRSCLLPQLHPQPDSGPQGRLPedvllKELELVQNAFFTDPNDQSAWFYHRW 234
Cdd:COG5536 161 FnfsdlKHELEYTTSLIETDIYNNSAWHHRYIWIERRFNRGDVISQKYLE-----KELEYIFDKIFTDPDNQSVWGYLRG 235


                ...
gi 53828918 235 LLG 237
Cdd:COG5536 236 VSS 238
PLN02789 PLN02789
farnesyltranstransferase
 40-250 1.17e-22

farnesyltranstransferase


Pssm-ID: 215423 [Multi-domain]  Cd Length: 320  Bit Score: 99.05  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   40 QAGELDESVLELTSQILGANPDFATLWNCRREVLQQLETQkspeelaalVKAELGFLESCLRVNPKSYGTWHHRCWLLGR 119
Cdd:PLN02789  48 ASDERSPRALDLTADVIRLNPGNYTVWHFRRLCLEALDAD---------LEEELDFAEDVAEDNPKNYQIWHHRRWLAEK 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918  120 LPEPNWTRELELCARFLEVDERNFHCWDYRRFVaTQAAVPPAEELAFTDSLITRNFSNYSSWHYR------SCLLPQLHP 193
Cdd:PLN02789 119 LGPDAANKELEFTRKILSLDAKNYHAWSHRQWV-LRTLGGWEDELEYCHQLLEEDVRNNSAWNQRyfvitrSPLLGGLEA 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 53828918  194 QPDSgpqgrlpedvllkELELVQNAFFTDPNDQSAWFYHRWLLGR------ADPQDALRCLHV 250
Cdd:PLN02789 198 MRDS-------------ELKYTIDAILANPRNESPWRYLRGLFKDdkealvSDPEVSSVCLEV 247
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 444-547 8.64e-14

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: 70.59  E-value: 8.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 444 RVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLR---TL---PPALAAL-RCLEVLQASDNAIESLDGVTNLPRLQELLLC 516
Cdd:cd21340  71 KKLYLGGNRISVVEGLENLTNLEELHIENQRLPpgeKLtfdPRSLAALsNSLRVLNISGNNIDSLEPLAPLRNLEQLDAS 150

                        90       100       110
                ....*....|....*....|....*....|..
gi 53828918 517 NNRLQQ-PAVLQPLASCPRLVLLNLQGNPLCQ 547
Cdd:cd21340 151 NNQISDlEELLDLLSSWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
444-545 3.86e-12

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 68.42  E-value: 3.86e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 444 RVLHLAHKDLTVL-CHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLQQ 522
Cdd:COG4886 185 KELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTD 264

                        90       100
                ....*....|....*....|...
gi 53828918 523 pavLQPLASCPRLVLLNLQGNPL 545
Cdd:COG4886 265 ---LPPLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
351-558 2.81e-11

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.73  E-value: 2.81e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 351 LFRCELSVEKSTVLQSELESCKELQELEPENKWCLLTIILLMRALDPLLYEKETLQYFQTLKAVDPMRATYLDDLRSKFL 430
Cdd:COG4886   2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 431 LENSVLKMEYAEvRVLHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPPALAALRCLEVLQASDNAIESL-DGVTNLPR 509
Cdd:COG4886  82 LSLLLLGLTDLG-DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLpEPLGNLTN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 53828918 510 LQELLLCNNRLQQ-PAvlqPLASCPRLVLLNLQGNPLCQAVGILEQLAEL 558
Cdd:COG4886 161 LKSLDLSNNQLTDlPE---ELGNLTNLKELDLSNNQITDLPEPLGNLTNL 207
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 446-559 3.61e-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: 3.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918 446 LHLAHKDLTVLCHLEQLLLVTHLDLSHNRLRTLPpALAALRCLEVLQASDNAIESLDGVTNLPRLQELLLCNNRLqqpAV 525
Cdd:cd21340   7 LYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRI---SV 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 53828918 526 LQPLASCPRLVLLNLQ------GNPLCQAVGILEQLAELL 559
Cdd:cd21340  83 VEGLENLTNLEELHIEnqrlppGEKLTFDPRSLAALSNSL 122
LRR_9 pfam14580
Leucine-rich repeat;
468-545 1.03e-05

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 46.30  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   468 LDLSHNRLRTLPpALAALRCLEVLQASDNAI----ESLDGVtnLPRLQELLLCNNRLQQPAVLQPLASCPRLVLLNLQGN 543
Cdd:pfam14580  47 IDFSDNEIRKLD-GFPLLRRLKTLLLNNNRIcrigEGLGEA--LPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRN 123


                  ..
gi 53828918   544 PL 545
Cdd:pfam14580 124 PV 125
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 162-191 4.11e-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: 40.70  E-value: 4.11e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 53828918   162 EELAFTDSLITRNFSNYSSWHYRSCLLPQL 191
Cdd:pfam01239   3 EELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 89-120 3.60e-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: 38.00  E-value: 3.60e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 53828918    89 VKAELGFLESCLRVNPKSYGTWHHRCWLLGRL 120
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLERL 32
PPTA pfam01239
Protein prenyltransferase alpha subunit repeat; Both farnesyltransferase (FT) and ...
 208-238 6.25e-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: 6.25e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 53828918   208 LLKELELVQNAFFTDPNDQSAWFYHRWLLGR 238
Cdd:pfam01239   1 LEEELALTDKLLELNPKNYSAWNHRRWLLER 31
LRR_8 pfam13855
Leucine rich repeat;
442-498 7.74e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 7.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 53828918   442 EVRVLHLAHKDLTVLC--HLEQLLLVTHLDLSHNRLRTLPP-ALAALRCLEVLQASDNAI 498
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDdgAFKGLSNLKVLDLSNNLLTTLSPgAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
488-545 1.33e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 1.33e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 53828918   488 LEVLQASDNAIESLDGVT--NLPRLQELLLCNNRLQQ--PAVLQPLascPRLVLLNLQGNPL 545
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAfkGLSNLKVLDLSNNLLTTlsPGAFSGL---PSLRYLDLSGNRL 61
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 508-554 4.63e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 35.30  E-value: 4.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 53828918   508 PRLQELLLCNNRLQqpaVLQPLASCPRLVLLNLQGNPLCQAVGILEQ 554
Cdd:pfam12799   1 PNLEVLDLSNNQIT---DIPPLAKLPNLETLDLSGNNKITDLSDLAN 44
 
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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