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Conserved domains on  [gi|119627333|gb|EAX06928|]
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leucine rich repeat containing 41, isoform CRA_b [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1903219)

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

CATH:  3.80.10.10
Gene Ontology:  GO:0005515
SCOP:  4003523

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
442-702 3.24e-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.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 43.50  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 442 GSDPSCLGLpALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWvSLESLTLSYNGLGSNIFRLL-DSLRALSgqagC 520
Cdd:cd00116   64 GRIPRGLQS-LLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLP----P 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 521 RLRALHLSD-LFSPLPILELTRAIvRALPLLRVLSIRvdhpsqrDNPgvpgnagppshiIGDEEIPEYNLALKRLS-FHD 598
Cdd:cd00116  138 ALEKLVLGRnRLEGASCEALAKAL-RANRDLKELNLA-------NNG------------IGDAGIRALAEGLKANCnLEV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 599 MNLADCQ---------SEVLflLQNLTLQEITFSFCRLFEKRPAQFLPEMvaaMKGNSTLKGLRLPGNRLGNAGLLALAD 669
Cdd:cd00116  198 LDLNNNGltdegasalAETL--ASLKSLEVLNLGDNNLTDAGAAALASAL---LSPNISLLTLSLSCNDITDDGAKDLAE 272
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119627333 670 VFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 702
Cdd:cd00116  273 VLAE--KESLLELDLRGNKFGEEGAQLLAESLL 303
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
442-702 3.24e-04

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: 43.50  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 442 GSDPSCLGLpALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWvSLESLTLSYNGLGSNIFRLL-DSLRALSgqagC 520
Cdd:cd00116   64 GRIPRGLQS-LLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLP----P 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 521 RLRALHLSD-LFSPLPILELTRAIvRALPLLRVLSIRvdhpsqrDNPgvpgnagppshiIGDEEIPEYNLALKRLS-FHD 598
Cdd:cd00116  138 ALEKLVLGRnRLEGASCEALAKAL-RANRDLKELNLA-------NNG------------IGDAGIRALAEGLKANCnLEV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 599 MNLADCQ---------SEVLflLQNLTLQEITFSFCRLFEKRPAQFLPEMvaaMKGNSTLKGLRLPGNRLGNAGLLALAD 669
Cdd:cd00116  198 LDLNNNGltdegasalAETL--ASLKSLEVLNLGDNNLTDAGAAALASAL---LSPNISLLTLSLSCNDITDDGAKDLAE 272
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119627333 670 VFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 702
Cdd:cd00116  273 VLAE--KESLLELDLRGNKFGEEGAQLLAESLL 303
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
642-702 8.98e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 42.47  E-value: 8.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119627333 642 AMKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 702
Cdd:COG5238  287 ALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG--NKTLHTLNLAYNGIGAQGAIALAKALQ 345
 
Name Accession Description Interval E-value
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
442-702 3.24e-04

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: 43.50  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 442 GSDPSCLGLpALEASQRFRSISTLELFTVPLSTEAALTLCHLLSSWvSLESLTLSYNGLGSNIFRLL-DSLRALSgqagC 520
Cdd:cd00116   64 GRIPRGLQS-LLQGLTKGCGLQELDLSDNALGPDGCGVLESLLRSS-SLQELKLNNNGLGDRGLRLLaKGLKDLP----P 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 521 RLRALHLSD-LFSPLPILELTRAIvRALPLLRVLSIRvdhpsqrDNPgvpgnagppshiIGDEEIPEYNLALKRLS-FHD 598
Cdd:cd00116  138 ALEKLVLGRnRLEGASCEALAKAL-RANRDLKELNLA-------NNG------------IGDAGIRALAEGLKANCnLEV 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 599 MNLADCQ---------SEVLflLQNLTLQEITFSFCRLFEKRPAQFLPEMvaaMKGNSTLKGLRLPGNRLGNAGLLALAD 669
Cdd:cd00116  198 LDLNNNGltdegasalAETL--ASLKSLEVLNLGDNNLTDAGAAALASAL---LSPNISLLTLSLSCNDITDDGAKDLAE 272
                        250       260       270
                 ....*....|....*....|....*....|...
gi 119627333 670 VFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 702
Cdd:cd00116  273 VLAE--KESLLELDLRGNKFGEEGAQLLAESLL 303
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
642-702 8.98e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 42.47  E-value: 8.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119627333 642 AMKGNSTLKGLRLPGNRLGNAGLLALADVFSEdsSSSLCQLDISSNCIKPDGLLEFAKRLE 702
Cdd:COG5238  287 ALQGNTTLTSLDLSVNRIGDEGAIALAEGLQG--NKTLHTLNLAYNGIGAQGAIALAKALQ 345
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
611-702 4.72e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 40.16  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 611 LLQNLTLQEITFSFCRLFEKRpAQFLpemVAAMKGNSTLKGLRLPGNRLGNAGLLALADvfSEDSSSSLCQLDISSNCIK 690
Cdd:COG5238  316 LQGNKTLHTLNLAYNGIGAQG-AIAL---AKALQENTTLHSLDLSDNQIGDEGAIALAK--YLEGNTTLRELNLGKNNIG 389
                         90
                 ....*....|..
gi 119627333 691 PDGLLEFAKRLE 702
Cdd:COG5238  390 KQGAEALIDALQ 401
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
448-736 5.46e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.92  E-value: 5.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 448 LGLPALEASQRFRSISTLELFTVPLSTeaaltLCHLLSSWVSLESLTLSYNG---LGSNIFRlLDSLRALSgqagcrLRA 524
Cdd:COG4886  101 LDLSGNEELSNLTNLESLDLSGNQLTD-----LPEELANLTNLKELDLSNNQltdLPEPLGN-LTNLKSLD------LSN 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 525 LHLSDLfsPLPILELTRaivralplLRVLSIrvdhpsqRDNPgvpgnagppshiIGDEEIPEYNL-ALKRLsfhdmNLAD 603
Cdd:COG4886  169 NQLTDL--PEELGNLTN--------LKELDL-------SNNQ------------ITDLPEPLGNLtNLEEL-----DLSG 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119627333 604 CQ-SEVLFLLQNLT-LQEITFSFCRLFEkrpaqfLPEmvaaMKGNSTLKGLRLPGNRlgnagllaLADVFSEDSSSSLCQ 681
Cdd:COG4886  215 NQlTDLPEPLANLTnLETLDLSNNQLTD------LPE----LGNLTNLEELDLSNNQ--------LTDLPPLANLTNLKT 276
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119627333 682 LDISSNCIKPDGL--LEFAKRLERWGRGAFGHLRLFQNWLDQDAVTAREAIRRLRAT 736
Cdd:COG4886  277 LDLSNNQLTDLKLkeLELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGL 333
 
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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