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Conserved domains on  [gi|185177518|pdb|2JQD|A]
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Chain A, Acidic leucine-rich nuclear phosphoprotein 32 family member A

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;
70-151 1.82e-07

Leucine-rich repeat;


The actual alignment was detected with superfamily member pfam14580:

Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 48.22  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2JQD_A         70 KLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMY 149
Cdd:pfam14580  65 RLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRL 144

                  ..
2JQD_A        150 LD 151
Cdd:pfam14580 145 LD 146
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
70-151 1.82e-07

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 48.22  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2JQD_A         70 KLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMY 149
Cdd:pfam14580  65 RLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRL 144

                  ..
2JQD_A        150 LD 151
Cdd:pfam14580 145 LD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-133 1.72e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 1.72e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2JQD_A       76 LSENRISGDLEVLAeKCPNLKHLNLSGNKIKDLStiEPLKKLENLKSLDLFNCEVTNL 133
Cdd:COG4886 143 LSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELDLSNNQITDL 197
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
75-140 3.65e-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: 45.16  E-value: 3.65e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2JQD_A       75 ELSENRISgDLEVLAeKCPNLKHLNLSGNKIKDLSTI-EPLKKLENLKSLDLFNCEVTNLNAYRENV 140
Cdd:cd21340 126 NISGNNID-SLEPLA-PLRNLEQLDASNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKPKYRDKI 190
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
70-151 1.82e-07

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 48.22  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2JQD_A         70 KLKKLELSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEPLKKLENLKSLDLFNCEVTNLNAYRENVFKLLPQVMY 149
Cdd:pfam14580  65 RLKTLLLNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRL 144

                  ..
2JQD_A        150 LD 151
Cdd:pfam14580 145 LD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-133 1.72e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 1.72e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2JQD_A       76 LSENRISGDLEVLAeKCPNLKHLNLSGNKIKDLStiEPLKKLENLKSLDLFNCEVTNL 133
Cdd:COG4886 143 LSNNQLTDLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELDLSNNQITDL 197
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
75-140 3.65e-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: 45.16  E-value: 3.65e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
2JQD_A       75 ELSENRISgDLEVLAeKCPNLKHLNLSGNKIKDLSTI-EPLKKLENLKSLDLFNCEVTNLNAYRENV 140
Cdd:cd21340 126 NISGNNID-SLEPLA-PLRNLEQLDASNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKPKYRDKI 190
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
25-133 1.72e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 1.72e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2JQD_A       25 KELVLDNCKsiegkIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKL----ELSENRISgDLEVLAEKCPNLKHLNL 100
Cdd:COG4886 139 KELDLSNNQ-----LTDLPEPLGNLTNLKSLDLSNNQLTDLPEELGNLTNlkelDLSNNQIT-DLPEPLGNLTNLEELDL 212
                        90       100       110
                ....*....|....*....|....*....|...
2JQD_A      101 SGNKIKDLStiEPLKKLENLKSLDLFNCEVTNL 133
Cdd:COG4886 213 SGNQLTDLP--EPLANLTNLETLDLSNNQLTDL 243
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-134 3.15e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 3.15e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
2JQD_A       76 LSENRISgDLEVLAeKCPNLKHLNLSGNKIKDLStiePLKKLENLKSLDLFNCEVTNLN 134
Cdd:COG4886 235 LSNNQLT-DLPELG-NLTNLEELDLSNNQLTDLP---PLANLTNLKTLDLSNNQLTDLK 288
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
93-128 3.32e-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: 39.54  E-value: 3.32e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
2JQD_A         93 PNLKHLNLSGNKIKDlstIEPLKKLENLKSLDLFNC 128
Cdd:pfam12799   1 PNLEVLDLSNNQITD---IPPLAKLPNLETLDLSGN 33
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
76-133 5.88e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 42.23  E-value: 5.88e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2JQD_A       76 LSENRISgDLEVLAEKCPNLKHLNLSGNKIKDLSTiepLKKLENLKSLDLFNCEVTNL 133
Cdd:COG4886 212 LSGNQLT-DLPEPLANLTNLETLDLSNNQLTDLPE---LGNLTNLEELDLSNNQLTDL 265
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
93-150 1.06e-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: 1.06e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
2JQD_A       93 PNLKHLNLSGNKIkdlSTIEPLKKLENLKSLDLFNCEVTNLnayrENVFKLLPQVMYL 150
Cdd:cd21340 120 NSLRVLNISGNNI---DSLEPLAPLRNLEQLDASNNQISDL----EELLDLLSSWPSL 170
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
78-133 6.77e-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: 39.34  E-value: 6.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
2JQD_A         78 ENRISGDLEVLAEKCPNLKHLNLSG-------NKIKDLSTIepLKKLENLKSLDLFNCEVTNL 133
Cdd:pfam19729 285 DDIDSSIVETLVACCPNLRHLNLSAahhhsseGLGGHLCAL--LARLKHLRSLSLPVCAVADS 345
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
33-135 9.22e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 38.76  E-value: 9.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2JQD_A       33 KSIEGKIEGLTDEFEELEFLSTINVGLTSISNLPKLNKLKKLELSENRISGDLEVlaEKCPNLKHLNLSGNKIKDLStiE 112
Cdd:COG4886  55 LLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEEL--SNLTNLESLDLSGNQLTDLP--E 130
                        90       100
                ....*....|....*....|...
2JQD_A      113 PLKKLENLKSLDLFNCEVTNLNA 135
Cdd:COG4886 131 ELANLTNLKELDLSNNQLTDLPE 153
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
88-131 1.95e-03

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: 37.31  E-value: 1.95e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
2JQD_A       88 LAEKCPNLKHLNL----SGNKIKDLSTIEPLKKLENLKSLDLFNCEVT 131
Cdd:cd09293  99 LATNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVT 146
LRR_8 pfam13855
Leucine rich repeat;
93-151 5.07e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 34.04  E-value: 5.07e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
2JQD_A         93 PNLKHLNLSGNKIKDLSTiEPLKKLENLKSLDLFNcevTNLNAYRENVFKLLPQVMYLD 151
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDD-GAFKGLSNLKVLDLSN---NLLTTLSPGAFSGLPSLRYLD 55
LRR_8 pfam13855
Leucine rich repeat;
76-128 5.44e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 33.65  E-value: 5.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
2JQD_A         76 LSENRISGDLEVLAEKCPNLKHLNLSGNKIKDLSTIEpLKKLENLKSLDLFNC 128
Cdd:pfam13855   8 LSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGA-FSGLPSLRYLDLSGN 59
 
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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