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Conserved domains on  [gi|967497285|ref|XP_014979038|]
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leucine-rich repeat LGI family member 4 isoform X4 [Macaca mulatta]

Protein Classification

LRR_8 and EPTP domain-containing protein( domain architecture ID 12158096)

LRR_8 and EPTP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR_8 pfam13855
Leucine rich repeat;
76-136 2.84e-15

Leucine rich repeat;


:

Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 70.25  E-value: 2.84e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967497285   76 PSLHLLLFTSNSFSVIEDDAFAGLSHLQYLFIEDNEIGSISKNALRGLRSLTHLSLANNHL 136
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 396-437 1.88e-08

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


:

Pssm-ID: 461033  Cd Length: 41  Bit Score: 50.16  E-value: 1.88e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 967497285  396 RFERRTDIPEAeDVYATRHFQAGGDVFLCLTRYIGDSMVMRW 437
Cdd:pfam03736   1 KFVPYQTIPTR-GARDVEPFSIGGDLFLAVANFSGDSVIYRW 41
PCC super family cl28216
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 131-206 2.17e-08

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


The actual alignment was detected with superfamily member TIGR00864:

Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 57.40  E-value: 2.17e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967497285   131 LANNHLEALPRFLFRGLETLTHVDLRGNPFQCDCRVLWLLQWMPTVNASV---GTGACAGPAALSHMQLRHLDPETFKC 206
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVrqpEAALCAGPGALAGQPLLGIPLLDSGC 80
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 351-392 3.62e-05

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


:

Pssm-ID: 461033  Cd Length: 41  Bit Score: 40.91  E-value: 3.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 967497285  351 GFYPHQSLHAWhRDTDAEALELDGRPHLLLASASQRPVLFHW 392
Cdd:pfam03736   1 KFVPYQTIPTR-GARDVEPFSIGGDLFLAVANFSGDSVIYRW 41
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 214-250 1.73e-04

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


:

Pssm-ID: 461033  Cd Length: 41  Bit Score: 38.99  E-value: 1.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 967497285  214 FQTV-GESALSVEPFSYEGEPHIVLAqPFAGRCLILSW 250
Cdd:pfam03736   5 YQTIpTRGARDVEPFSIGGDLFLAVA-NFSGDSVIYRW 41
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 441-480 7.33e-04

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


:

Pssm-ID: 461033  Cd Length: 41  Bit Score: 37.45  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 967497285  441 MFRLLQQLPSRGAHVFQPLLIARDQLAILGSDFAFSQVLR 480
Cdd:pfam03736   1 KFVPYQTIPTRGARDVEPFSIGGDLFLAVANFSGDSVIYR 40
 
Name Accession Description Interval E-value
LRR_8 pfam13855
Leucine rich repeat;
76-136 2.84e-15

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 70.25  E-value: 2.84e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967497285   76 PSLHLLLFTSNSFSVIEDDAFAGLSHLQYLFIEDNEIGSISKNALRGLRSLTHLSLANNHL 136
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-160 1.33e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.74  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967497285  45 DLPVSFS--PNLLSLSFVRTGVTQLKAgSFLRIPSLHLLLFTSNSFSVIEDdAFAGLSHLQYLFIEDNEIGSISKnALRG 122
Cdd:COG4886  150 DLPEPLGnlTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDLPE-PLAN 226

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 967497285 123 LRSLTHLSLANNHLEALPRFLfrGLETLTHVDLRGNPF 160
Cdd:COG4886  227 LTNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQL 262
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 396-437 1.88e-08

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 50.16  E-value: 1.88e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 967497285  396 RFERRTDIPEAeDVYATRHFQAGGDVFLCLTRYIGDSMVMRW 437
Cdd:pfam03736   1 KFVPYQTIPTR-GARDVEPFSIGGDLFLAVANFSGDSVIYRW 41
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 131-206 2.17e-08

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 57.40  E-value: 2.17e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967497285   131 LANNHLEALPRFLFRGLETLTHVDLRGNPFQCDCRVLWLLQWMPTVNASV---GTGACAGPAALSHMQLRHLDPETFKC 206
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVrqpEAALCAGPGALAGQPLLGIPLLDSGC 80
LRRCT smart00082
Leucine rich repeat C-terminal domain;
158-206 3.66e-07

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 47.04  E-value: 3.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 967497285   158 NPFQCDCRVLWLLQWMPTVNASVGTGA--CAGPAALsHMQLRHLDPETFKC 206
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVDlrCASPSSL-RGPLLELLHSEFKC 50
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 91-160 2.64e-06

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: 48.63  E-value: 2.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967497285  91 IEDDAFAGLSH-LQYLFIEDNEIGSISKnaLRGLRSLTHLSLANNHLEALPRF--LFRGLETLTHVDLRGNPF 160
Cdd:cd21340  110 FDPRSLAALSNsLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEELldLLSSWPSLRELDLTGNPV 180
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 351-392 3.62e-05

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 40.91  E-value: 3.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 967497285  351 GFYPHQSLHAWhRDTDAEALELDGRPHLLLASASQRPVLFHW 392
Cdd:pfam03736   1 KFVPYQTIPTR-GARDVEPFSIGGDLFLAVANFSGDSVIYRW 41
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 214-250 1.73e-04

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 38.99  E-value: 1.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 967497285  214 FQTV-GESALSVEPFSYEGEPHIVLAqPFAGRCLILSW 250
Cdd:pfam03736   5 YQTIpTRGARDVEPFSIGGDLFLAVA-NFSGDSVIYRW 41
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 441-480 7.33e-04

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 37.45  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 967497285  441 MFRLLQQLPSRGAHVFQPLLIARDQLAILGSDFAFSQVLR 480
Cdd:pfam03736   1 KFVPYQTIPTRGARDVEPFSIGGDLFLAVANFSGDSVIYR 40
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 125-167 1.22e-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: 36.84  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 967497285  125 SLTHLSLANNHLEALPrfLFRGLETLTHVDLRGNPFQCDCRVL 167
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNKITDLSDL 42
LRR smart00370
Leucine-rich repeats, outliers;
123-146 2.54e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 2.54e-03
                           10        20
                   ....*....|....*....|....
gi 967497285   123 LRSLTHLSLANNHLEALPRFLFRG 146
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQG 24
 
Name Accession Description Interval E-value
LRR_8 pfam13855
Leucine rich repeat;
76-136 2.84e-15

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 70.25  E-value: 2.84e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967497285   76 PSLHLLLFTSNSFSVIEDDAFAGLSHLQYLFIEDNEIGSISKNALRGLRSLTHLSLANNHL 136
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-160 1.33e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 75.74  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967497285  45 DLPVSFS--PNLLSLSFVRTGVTQLKAgSFLRIPSLHLLLFTSNSFSVIEDdAFAGLSHLQYLFIEDNEIGSISKnALRG 122
Cdd:COG4886  150 DLPEPLGnlTNLKSLDLSNNQLTDLPE-ELGNLTNLKELDLSNNQITDLPE-PLGNLTNLEELDLSGNQLTDLPE-PLAN 226

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 967497285 123 LRSLTHLSLANNHLEALPRFLfrGLETLTHVDLRGNPF 160
Cdd:COG4886  227 LTNLETLDLSNNQLTDLPELG--NLTNLEELDLSNNQL 262
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-160 2.80e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.97  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967497285  45 DLPVSFS--PNLLSLSFVRTGVTQLKAgSFLRIPSLHLLLFTSNSFSVIeDDAFAGLSHLQYLFIEDNEIGSISKnALRG 122
Cdd:COG4886  127 DLPEELAnlTNLKELDLSNNQLTDLPE-PLGNLTNLKSLDLSNNQLTDL-PEELGNLTNLKELDLSNNQITDLPE-PLGN 203

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 967497285 123 LRSLTHLSLANNHLEALPRFLfRGLETLTHVDLRGNPF 160
Cdd:COG4886  204 LTNLEELDLSGNQLTDLPEPL-ANLTNLETLDLSNNQL 240
LRR_8 pfam13855
Leucine rich repeat;
100-160 5.82e-10

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 55.22  E-value: 5.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967497285  100 SHLQYLFIEDNEIGSISKNALRGLRSLTHLSLANNHLEALPRFLFRGLETLTHVDLRGNPF 160
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 396-437 1.88e-08

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 50.16  E-value: 1.88e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 967497285  396 RFERRTDIPEAeDVYATRHFQAGGDVFLCLTRYIGDSMVMRW 437
Cdd:pfam03736   1 KFVPYQTIPTR-GARDVEPFSIGGDLFLAVANFSGDSVIYRW 41
PCC TIGR00864
polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) ...
 131-206 2.17e-08

polycystin cation channel protein; The Polycystin Cation Channel (PCC) Family (TC 1.A.5) Polycystin is a huge protein of 4303aas. Its repeated leucine-rich (LRR) segment is found in many proteins. It contains 16 polycystic kidney disease (PKD) domains, one LDL-receptor class A domain, one C-type lectin family domain, and 16-18 putative TMSs in positions between residues 2200 and 4100. Polycystin-L has been shown to be a cation (Na+, K+ and Ca2+) channel that is activated by Ca2+. Two members of the PCC family (polycystin 1 and 2) are mutated in autosomal dominant polycystic kidney disease, and polycystin-L is deleted in mice with renal and retinal defects. Note: this model is restricted to the amino half.


Pssm-ID: 188093 [Multi-domain]  Cd Length: 2740  Bit Score: 57.40  E-value: 2.17e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967497285   131 LANNHLEALPRFLFRGLETLTHVDLRGNPFQCDCRVLWLLQWMPTVNASV---GTGACAGPAALSHMQLRHLDPETFKC 206
Cdd:TIGR00864    2 ISNNKISTIEEGICANLCNLSEIDLSGNPFECDCGLARLPRWAEEKGVKVrqpEAALCAGPGALAGQPLLGIPLLDSGC 80
LRRCT smart00082
Leucine rich repeat C-terminal domain;
158-206 3.66e-07

Leucine rich repeat C-terminal domain;


Pssm-ID: 214507 [Multi-domain]  Cd Length: 51  Bit Score: 47.04  E-value: 3.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 967497285   158 NPFQCDCRVLWLLQWMPTVNASVGTGA--CAGPAALsHMQLRHLDPETFKC 206
Cdd:smart00082   1 NPFICDCELRWLLRWLQANEHLQDPVDlrCASPSSL-RGPLLELLHSEFKC 50
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-139 4.83e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 4.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967497285  45 DLPVSFS--PNLLSLSFVRTGVTQLKAgSFLRIPSLHLLLFTSNSFSVIEDdaFAGLSHLQYLFIEDNEIGSISKNAlrG 122
Cdd:COG4886  196 DLPEPLGnlTNLEELDLSGNQLTDLPE-PLANLTNLETLDLSNNQLTDLPE--LGNLTNLEELDLSNNQLTDLPPLA--N 270

                         90
                 ....*....|....*..
gi 967497285 123 LRSLTHLSLANNHLEAL 139
Cdd:COG4886  271 LTNLKTLDLSNNQLTDL 287
LRR_8 pfam13855
Leucine rich repeat;
52-112 9.56e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.98  E-value: 9.56e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 967497285   52 PNLLSLSFVRTGVTQLKAGSFLRIPSLHLLLFTSNSFSVIEDDAFAGLSHLQYLFIEDNEI 112
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 91-160 2.64e-06

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: 48.63  E-value: 2.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967497285  91 IEDDAFAGLSH-LQYLFIEDNEIGSISKnaLRGLRSLTHLSLANNHLEALPRF--LFRGLETLTHVDLRGNPF 160
Cdd:cd21340  110 FDPRSLAALSNsLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEELldLLSSWPSLRELDLTGNPV 180
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 351-392 3.62e-05

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 40.91  E-value: 3.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 967497285  351 GFYPHQSLHAWhRDTDAEALELDGRPHLLLASASQRPVLFHW 392
Cdd:pfam03736   1 KFVPYQTIPTR-GARDVEPFSIGGDLFLAVANFSGDSVIYRW 41
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 214-250 1.73e-04

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 38.99  E-value: 1.73e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 967497285  214 FQTV-GESALSVEPFSYEGEPHIVLAqPFAGRCLILSW 250
Cdd:pfam03736   5 YQTIpTRGARDVEPFSIGGDLFLAVA-NFSGDSVIYRW 41
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
80-160 1.75e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.15  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967497285  80 LLLFTSNSFSVIEDDAFAGLSHLQYLFIEDNeigsiskNALRGLRSLTHLSLANNHLEALPRFLFRgLETLTHVDLRGNP 159
Cdd:COG4886   76 LLSLLLLSLLLLGLTDLGDLTNLTELDLSGN-------EELSNLTNLESLDLSGNQLTDLPEELAN-LTNLKELDLSNNQ 147


                 .
gi 967497285 160 F 160
Cdd:COG4886  148 L 148
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 76-142 2.22e-04

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: 42.85  E-value: 2.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 967497285  76 PSLHLLLFTSNSFSVIEDdaFAGLSHLQYLFIEDNEIGSIS--KNALRGLRSLTHLSLANNHLEALPRF 142
Cdd:cd21340  120 NSLRVLNISGNNIDSLEP--LAPLRNLEQLDASNNQISDLEelLDLLSSWPSLRELDLTGNPVCKKPKY 186
EPTP pfam03736
EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, ...
 441-480 7.33e-04

EPTP domain; Mutations in the LGI/Epitempin gene can result in a special form of epilepsy, autosomal dominant lateral temporal epilepsy. The Epitempin protein contains a large repeat in its C terminal section. The architecture and structural features of this repeat make it a likely member 7-bladed beta-propeller fold.


Pssm-ID: 461033  Cd Length: 41  Bit Score: 37.45  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 967497285  441 MFRLLQQLPSRGAHVFQPLLIARDQLAILGSDFAFSQVLR 480
Cdd:pfam03736   1 KFVPYQTIPTRGARDVEPFSIGGDLFLAVANFSGDSVIYR 40
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 125-167 1.22e-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: 36.84  E-value: 1.22e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 967497285  125 SLTHLSLANNHLEALPrfLFRGLETLTHVDLRGNPFQCDCRVL 167
Cdd:pfam12799   2 NLEVLDLSNNQITDIP--PLAKLPNLETLDLSGNNKITDLSDL 42
LRR smart00370
Leucine-rich repeats, outliers;
123-146 2.54e-03

Leucine-rich repeats, outliers;


Pssm-ID: 197688 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 2.54e-03
                           10        20
                   ....*....|....*....|....
gi 967497285   123 LRSLTHLSLANNHLEALPRFLFRG 146
Cdd:smart00370   1 LPNLRELDLSNNQLSSLPPGAFQG 24
LRR_TYP smart00369
Leucine-rich repeats, typical (most populated) subfamily;
123-146 2.54e-03

Leucine-rich repeats, typical (most populated) subfamily;


Pssm-ID: 197687 [Multi-domain]  Cd Length: 24  Bit Score: 35.41  E-value: 2.54e-03
                           10        20
                   ....*....|....*....|....
gi 967497285   123 LRSLTHLSLANNHLEALPRFLFRG 146
Cdd:smart00369   1 LPNLRELDLSNNQLSSLPPGAFQG 24
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 99-158 3.63e-03

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: 39.00  E-value: 3.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 967497285  99 LSHLqYLFieDNEIGSISKnaLRGLRSLTHLSLANNHLEALPRflFRGLETLTHVDLRGN 158
Cdd:cd21340   26 LKVL-YLY--DNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN--LENLVNLKKLYLGGN 78
 
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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