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Conserved domains on  [gi|67846084|ref|NP_001020073|]
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leucine-rich repeat-containing protein 56 [Rattus norvegicus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 11469232)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  11751054|7583641|14747988
SCOP:  4003523

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-292 3.11e-13

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  92 LPNLIQLKLNHSCLGSLRDLGTSLGQLQVLWLARCGLTDLDGIGSFLALKELYVSYNNISDLSPLCLLEQLEVLDLEGNN 171
Cdd:COG4886 204 LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQ 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084 172 VEDLgqmrylqlcpRLTTLTLEGNLVCLKPDPGPSNKAPQDYNYRAEVKKLIPQLHILDEVPTTCTNLPAPQKLSQDWLM 251
Cdd:COG4886 284 LTDL----------KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 67846084 252 VKEAIKEGNVLDILLPRLECSHGATIRKFDPTLPVPETQPW 292
Cdd:COG4886 354 LLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-292 3.11e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  92 LPNLIQLKLNHSCLGSLRDLGTSLGQLQVLWLARCGLTDLDGIGSFLALKELYVSYNNISDLSPLCLLEQLEVLDLEGNN 171
Cdd:COG4886 204 LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQ 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084 172 VEDLgqmrylqlcpRLTTLTLEGNLVCLKPDPGPSNKAPQDYNYRAEVKKLIPQLHILDEVPTTCTNLPAPQKLSQDWLM 251
Cdd:COG4886 284 LTDL----------KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 67846084 252 VKEAIKEGNVLDILLPRLECSHGATIRKFDPTLPVPETQPW 292
Cdd:COG4886 354 LLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 91-233 3.68e-13

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: 68.66  E-value: 3.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  91 HLPNLIQLKLNHSCLGSLRDLGtSLGQLQVLWLAR------CGLTDLDgigsflALKELYVSY----------------- 147
Cdd:cd21340  44 FLTNLTHLYLQNNQIEKIENLE-NLVNLKKLYLGGnrisvvEGLENLT------NLEELHIENqrlppgekltfdprsla 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084 148 -------------NNISDLSPLCLLEQLEVLDLEGNNVEDLGQM-RYLQLCPRLTTLTLEGNLVCLKPdpgpsnkapqdy 213
Cdd:cd21340 117 alsnslrvlnisgNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKP------------ 184

                       170       180
                ....*....|....*....|
gi 67846084 214 NYRAEVKKLIPQLHILDEVP 233
Cdd:cd21340 185 KYRDKIILASKSLEVLDGKE 204
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 140-171 1.02e-05

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: 42.62  E-value: 1.02e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 67846084   140 LKELYVSYNNISDLSPLCLLEQLEVLDLEGNN 171
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNN 34
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
92-292 3.11e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.11e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  92 LPNLIQLKLNHSCLGSLRDLGTSLGQLQVLWLARCGLTDLDGIGSFLALKELYVSYNNISDLSPLCLLEQLEVLDLEGNN 171
Cdd:COG4886 204 LTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQ 283

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084 172 VEDLgqmrylqlcpRLTTLTLEGNLVCLKPDPGPSNKAPQDYNYRAEVKKLIPQLHILDEVPTTCTNLPAPQKLSQDWLM 251
Cdd:COG4886 284 LTDL----------KLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLL 353

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 67846084 252 VKEAIKEGNVLDILLPRLECSHGATIRKFDPTLPVPETQPW 292
Cdd:COG4886 354 LLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLL 394
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
91-195 3.25e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 71.50  E-value: 3.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  91 HLPNLIQLKLNHSCLGSLRDLGTSLGQLQVLWLARCGLTDL-DGIGSFLALKELYVSYNNISDLS-PLCLLEQLEVLDLE 168
Cdd:COG4886 134 NLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLPePLGNLTNLEELDLS 213

                        90       100
                ....*....|....*....|....*..
gi 67846084 169 GNNVEDLGQmrYLQLCPRLTTLTLEGN 195
Cdd:COG4886 214 GNQLTDLPE--PLANLTNLETLDLSNN 238
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 91-233 3.68e-13

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: 68.66  E-value: 3.68e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  91 HLPNLIQLKLNHSCLGSLRDLGtSLGQLQVLWLAR------CGLTDLDgigsflALKELYVSY----------------- 147
Cdd:cd21340  44 FLTNLTHLYLQNNQIEKIENLE-NLVNLKKLYLGGnrisvvEGLENLT------NLEELHIENqrlppgekltfdprsla 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084 148 -------------NNISDLSPLCLLEQLEVLDLEGNNVEDLGQM-RYLQLCPRLTTLTLEGNLVCLKPdpgpsnkapqdy 213
Cdd:cd21340 117 alsnslrvlnisgNNIDSLEPLAPLRNLEQLDASNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKP------------ 184

                       170       180
                ....*....|....*....|
gi 67846084 214 NYRAEVKKLIPQLHILDEVP 233
Cdd:cd21340 185 KYRDKIILASKSLEVLDGKE 204
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 140-171 1.02e-05

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: 42.62  E-value: 1.02e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 67846084   140 LKELYVSYNNISDLSPLCLLEQLEVLDLEGNN 171
Cdd:pfam12799   3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGNN 34
LRR_8 pfam13855
Leucine rich repeat;
117-172 2.80e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 2.80e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 67846084   117 QLQVLWLARCGLTDLDGiGSFL---ALKELYVSYNNISDLSPLCL--LEQLEVLDLEGNNV 172
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDD-GAFKglsNLKVLDLSNNLLTTLSPGAFsgLPSLRYLDLSGNRL 61
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 117-156 6.12e-05

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: 40.31  E-value: 6.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 67846084   117 QLQVLWLARCGLTDLDGIGSFLALKELYVSYNN-ISDLSPL 156
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNNkITDLSDL 42
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 115-195 1.79e-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: 1.79e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084 115 LGQLQVLWLARCGLTDLDGIGSFLALKELYVSYNNISDLSPLCLLEQLEVLDLEGNNVEdlgQMRYLQLCPRLTTLTLEG 194
Cdd:cd21340   1 LKRITHLYLNDKNITKIDNLSLCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIE---KIENLENLVNLKKLYLGG 77


                .
gi 67846084 195 N 195
Cdd:cd21340  78 N 78
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 98-193 2.78e-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: 42.47  E-value: 2.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084  98 LKLNHSCLGSLRDLGtSLGQLQVLWLARCGLTDLDGIGSFLALKELYVSYNNISDLSPLCLLEQLEVLDLEGNN---VED 174
Cdd:cd21340   7 LYLNDKNITKIDNLS-LCKNLKVLYLYDNKITKIENLEFLTNLTHLYLQNNQIEKIENLENLVNLKKLYLGGNRisvVEG 85

                        90
                ....*....|....*....
gi 67846084 175 lgqmryLQLCPRLTTLTLE 193
Cdd:cd21340  86 ------LENLTNLEELHIE 98
LRR_9 pfam14580
Leucine-rich repeat;
110-230 4.58e-04

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 41.29  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084   110 DLGTSLGQLQVLWLARCGLTDLDGIGSFLALKELYVSYNNISDLSPLclLEQ----LEVLDLEGNNVEDLGQMRYLQLCP 185
Cdd:pfam14580  36 NLGATLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRICRIGEG--LGEalpnLTELILTNNNLQELGDLDPLASLK 113

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 67846084   186 RLTTLTLEGNLVCLKPdpgpsnkapqdyNYRAEVKKLIPQLHILD 230
Cdd:pfam14580 114 KLTFLSLLRNPVTNKP------------HYRLYVIYKVPQLRLLD 146
LRR_8 pfam13855
Leucine rich repeat;
140-197 5.24e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.27  E-value: 5.24e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 67846084   140 LKELYVSYNNISDLSPLCL--LEQLEVLDLEGNNVEDLGqMRYLQLCPRLTTLTLEGNLV 197
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFkgLSNLKVLDLSNNLLTTLS-PGAFSGLPSLRYLDLSGNRL 61
 
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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