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Conserved domains on  [gi|210147571|ref|NP_001129951|]
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acidic leucine-rich nuclear phosphoprotein 32 family member E isoform 3 [Homo sapiens]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 705725)

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

Gene Ontology:  GO:0005515
PubMed:  11751054

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRR_9 super family cl25994
Leucine-rich repeat;
5-98 1.67e-09

Leucine-rich repeat;


The actual alignment was detected with superfamily member pfam14580:

Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 55.15  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571    5 ELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYR 84
Cdd:pfam14580  53 EIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYR 132
                          90
                  ....*....|....
gi 210147571   85 ESIFELLQQITYLD 98
Cdd:pfam14580 133 LYVIYKVPQLRLLD 146
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
5-98 1.67e-09

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 55.15  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571    5 ELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYR 84
Cdd:pfam14580  53 EIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYR 132
                          90
                  ....*....|....
gi 210147571   85 ESIFELLQQITYLD 98
Cdd:pfam14580 133 LYVIYKVPQLRLLD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
12-80 3.16e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.24  E-value: 3.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 210147571  12 LPSLNKLRKLELSDNIISGGLEVLAeKCPNLTYLNLSGNKIKDLStvEALQNLKNLKSLDLFNCEITNL 80
Cdd:COG4886  132 LANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELDLSNNQITDL 197
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
5-78 2.91e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 43.47  E-value: 2.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 210147571   5 ELSSLAR-LPSLNKLrKLELSDNIISGGLEVLAEKCPNLTYLNL----SGNKIKDLSTVEALQNLKNLKSLDLFNCEIT 78
Cdd:cd09293   69 GLIALAQsCPNLQVL-DLRACENITDSGIVALATNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVT 146
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
1-72 4.17e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 37.91  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571   1 MANVELSSLAR------LPSL---NKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEaLQNLKNLKSLD 71
Cdd:PLN00113 451 MPSLQMLSLARnkffggLPDSfgsKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDE-LSSCKKLVSLD 529

                 .
gi 210147571  72 L 72
Cdd:PLN00113 530 L 530
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
5-98 1.67e-09

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 55.15  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571    5 ELSSLARLPSLNKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEALQNLKNLKSLDLFNCEITNLEDYR 84
Cdd:pfam14580  53 EIRKLDGFPLLRRLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYR 132
                          90
                  ....*....|....
gi 210147571   85 ESIFELLQQITYLD 98
Cdd:pfam14580 133 LYVIYKVPQLRLLD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
12-80 3.16e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 47.24  E-value: 3.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 210147571  12 LPSLNKLRKLELSDNIISGGLEVLAeKCPNLTYLNLSGNKIKDLStvEALQNLKNLKSLDLFNCEITNL 80
Cdd:COG4886  132 LANLTNLKELDLSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELDLSNNQITDL 197
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
5-78 2.91e-05

Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in Saccharomyces cerevisiae as a component of the Antagonist of MEN pathway (AMEN). The AMEN network is activated by MEN (mitotic exit network) via an active Cdc14, and in turn switches off MEN. Amn1 constitutes one of the alternative mechanisms by which MEN may be disrupted. Specifically, Amn1 binds Tem1 (Termination of M-phase, a GTPase that belongs to the RAS superfamily), and disrupts its association with Cdc15, the primary downstream target. Amn1 is a leucine-rich repeat (LRR) protein, with 12 repeats in the S. cerevisiae ortholog. As a negative regulator of the signal transduction pathway MEN, overexpression of AMN1 slows the growth of wild type cells. The function of the vertebrate members of this family has not been determined experimentally, they have fewer LRRs that determine the extent of this model.


Pssm-ID: 187754 [Multi-domain]  Cd Length: 226  Bit Score: 43.47  E-value: 2.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 210147571   5 ELSSLAR-LPSLNKLrKLELSDNIISGGLEVLAEKCPNLTYLNL----SGNKIKDLSTVEALQNLKNLKSLDLFNCEIT 78
Cdd:cd09293   69 GLIALAQsCPNLQVL-DLRACENITDSGIVALATNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVT 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
12-80 1.31e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.23  E-value: 1.31e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 210147571  12 LPSLNKLRKLELSDNIISGGLEVLAeKCPNLTYLNLSGNKIKDLstvEALQNLKNLKSLDLFNCEITNL 80
Cdd:COG4886  201 LGNLTNLEELDLSGNQLTDLPEPLA-NLTNLETLDLSNNQLTDL---PELGNLTNLEELDLSNNQLTDL 265
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
40-105 2.27e-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: 40.92  E-value: 2.27e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 210147571  40 PNLTYLNLSGNKIKDLstvEALQNLKNLKSLDLFNCEITNLEDyresIFELLQQITYLDGFDQEDN 105
Cdd:cd21340  120 NSLRVLNISGNNIDSL---EPLAPLRNLEQLDASNNQISDLEE----LLDLLSSWPSLRELDLTGN 178
LRR_8 pfam13855
Leucine rich repeat;
17-77 3.10e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 3.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 210147571   17 KLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTvEALQNLKNLKSLDLFNCEI 77
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSP-GAFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
16-99 3.21e-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: 40.54  E-value: 3.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571  16 NKLRKLELSDNIISGgLEVLAeKCPNLTYLNLSGNKIKDLSTV-EALQNLKNLKSLDLFNCEITNLEDYRESIFELLQQI 94
Cdd:cd21340  120 NSLRVLNISGNNIDS-LEPLA-PLRNLEQLDASNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKPKYRDKIILASKSL 197

                 ....*
gi 210147571  95 TYLDG 99
Cdd:cd21340  198 EVLDG 202
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
12-80 3.78e-04

F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from F-box/LRR repeat protein 18 (also known as F-box and leucine-rich repeat protein 18, FBXL18), associated with F-box domains. This protein is the substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex through its F-box and the LRR motifs mediate the protein-protein interactions required for the binding of the specific substrates by SCFs complexes.


Pssm-ID: 466163 [Multi-domain]  Cd Length: 594  Bit Score: 40.88  E-value: 3.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 210147571   12 LPSLNKLRKLElsDNIISGGLEVLAEKCPNLTYLNLSG-------NKIKDLSTVeaLQNLKNLKSLDLFNCEITNL 80
Cdd:pfam19729 274 LLPDSLLRKAE--DDIDSSIVETLVACCPNLRHLNLSAahhhsseGLGGHLCAL--LARLKHLRSLSLPVCAVADS 345
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
12-81 4.05e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 4.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571  12 LPSLNKLRKLELSDNIISGgLEVLAeKCPNLTYLNLSGNKIKDLSTveaLQNLKNLKSLDLFNCEITNLE 81
Cdd:COG4886  224 LANLTNLETLDLSNNQLTD-LPELG-NLTNLEELDLSNNQLTDLPP---LANLTNLKTLDLSNNQLTDLK 288
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
40-85 8.14e-04

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: 36.07  E-value: 8.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 210147571   40 PNLTYLNLSGNKIKDLstvEALQNLKNLKSLDL-FNCEITNLEDYRE 85
Cdd:pfam12799   1 PNLEVLDLSNNQITDI---PPLAKLPNLETLDLsGNNKITDLSDLAN 44
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
17-72 2.27e-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: 38.23  E-value: 2.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 210147571  17 KLRKLELSDNIIS-GGLEVLAEKCPN---LTYLNLSGNKIKD---LSTVEALQNLKNLKSLDL 72
Cdd:COG5238  237 SLTTLDLSNNQIGdEGVIALAEALKNnttVETLYLSGNQIGAegaIALAKALQGNTTLTSLDL 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
18-105 3.92e-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: 37.85  E-value: 3.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571  18 LRKLELSDNIISG-GLEVLAE---KCPNLTYLNLSGNKIKDLSTV---EALQNLKNLKSLDLFNCEITNLEdyRESIFEL 90
Cdd:COG5238  266 VETLYLSGNQIGAeGAIALAKalqGNTTLTSLDLSVNRIGDEGAIalaEGLQGNKTLHTLNLAYNGIGAQG--AIALAKA 343
                         90
                 ....*....|....*
gi 210147571  91 LQQITYLDGFDQEDN 105
Cdd:COG5238  344 LQENTTLHSLDLSDN 358
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
1-72 4.17e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 37.91  E-value: 4.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571   1 MANVELSSLAR------LPSL---NKLRKLELSDNIISGGLEVLAEKCPNLTYLNLSGNKIKDLSTVEaLQNLKNLKSLD 71
Cdd:PLN00113 451 MPSLQMLSLARnkffggLPDSfgsKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDE-LSSCKKLVSLD 529

                 .
gi 210147571  72 L 72
Cdd:PLN00113 530 L 530
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
5-72 5.69e-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: 36.69  E-value: 5.69e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 210147571   5 ELSSLARLPSLNKLRKLELSDNIISGgLEVLaEKCPNLTYLNLSGNKIkdlSTVEALQNLKNLKSLDL 72
Cdd:cd21340   35 KITKIENLEFLTNLTHLYLQNNQIEK-IENL-ENLVNLKKLYLGGNRI---SVVEGLENLTNLEELHI 97
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
16-98 6.28e-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: 37.08  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 210147571  16 NKLRKLELSDNIISG-GLEVLAE---KCPNLTYLNLSGNKIKDLSTV---EALQNLKNLKSLDLFNCEITNLEdyRESIF 88
Cdd:COG5238  320 KTLHTLNLAYNGIGAqGAIALAKalqENTTLHSLDLSDNQIGDEGAIalaKYLEGNTTLRELNLGKNNIGKQG--AEALI 397
                         90
                 ....*....|..
gi 210147571  89 ELLQ--QITYLD 98
Cdd:COG5238  398 DALQtnRLHTLI 409
 
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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