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Conserved domains on  [gi|62857821|ref|NP_001016746|]
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acidic leucine-rich nuclear phosphoprotein 32 family member A [Xenopus tropicalis]

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;
71-146 8.80e-09

Leucine-rich repeat;


The actual alignment was detected with superfamily member pfam14580:

Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 53.23  E-value: 8.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62857821    71 LSDNNISGGLEVLAEKCPNLTHLNLSGNRIKDLSTIEPLKKLEHLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLD 146
Cdd:pfam14580  71 LNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLD 146
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
71-146 8.80e-09

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 53.23  E-value: 8.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62857821    71 LSDNNISGGLEVLAEKCPNLTHLNLSGNRIKDLSTIEPLKKLEHLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLD 146
Cdd:pfam14580  71 LNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-146 8.01e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 8.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62857821   2 DMKKRIHLELRNRTP----ADVKELVLDNCrskegKIEGLTDEFEGLEFLSTINvclssianlpklnklkkleLSDNNIS 77
Cdd:COG4886  94 DLTNLTELDLSGNEElsnlTNLESLDLSGN-----QLTDLPEELANLTNLKELD-------------------LSNNQLT 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62857821  78 GGLEVLAeKCPNLTHLNLSGNRIKDLStiEPLKKLEHLKSLDLFNCEVTNLndyrENVFKLLPQLTYLD 146
Cdd:COG4886 150 DLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELDLSNNQITDL----PEPLGNLTNLEELD 211
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
88-146 1.02e-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: 47.86  E-value: 1.02e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62857821  88 PNLTHLNLSGNRIkdlSTIEPLKKLEHLKSLDLFNCEVTNLNDYrENVFKLLPQLTYLD 146
Cdd:cd21340 120 NSLRVLNISGNNI---DSLEPLAPLRNLEQLDASNNQISDLEEL-LDLLSSWPSLRELD 174
 
Name Accession Description Interval E-value
LRR_9 pfam14580
Leucine-rich repeat;
71-146 8.80e-09

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 53.23  E-value: 8.80e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62857821    71 LSDNNISGGLEVLAEKCPNLTHLNLSGNRIKDLSTIEPLKKLEHLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLD 146
Cdd:pfam14580  71 LNNNRICRIGEGLGEALPNLTELILTNNNLQELGDLDPLASLKKLTFLSLLRNPVTNKPHYRLYVIYKVPQLRLLD 146
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
2-146 8.01e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.24  E-value: 8.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62857821   2 DMKKRIHLELRNRTP----ADVKELVLDNCrskegKIEGLTDEFEGLEFLSTINvclssianlpklnklkkleLSDNNIS 77
Cdd:COG4886  94 DLTNLTELDLSGNEElsnlTNLESLDLSGN-----QLTDLPEELANLTNLKELD-------------------LSNNQLT 149
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62857821  78 GGLEVLAeKCPNLTHLNLSGNRIKDLStiEPLKKLEHLKSLDLFNCEVTNLndyrENVFKLLPQLTYLD 146
Cdd:COG4886 150 DLPEPLG-NLTNLKSLDLSNNQLTDLP--EELGNLTNLKELDLSNNQITDL----PEPLGNLTNLEELD 211
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
88-146 1.02e-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: 47.86  E-value: 1.02e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 62857821  88 PNLTHLNLSGNRIkdlSTIEPLKKLEHLKSLDLFNCEVTNLNDYrENVFKLLPQLTYLD 146
Cdd:cd21340 120 NSLRVLNISGNNI---DSLEPLAPLRNLEQLDASNNQISDLEEL-LDLLSSWPSLRELD 174
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
70-147 1.95e-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: 47.09  E-value: 1.95e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62857821  70 ELSDNNISGgLEVLAeKCPNLTHLNLSGNRIKDLSTI-EPLKKLEHLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLDG 147
Cdd:cd21340 126 NISGNNIDS-LEPLA-PLRNLEQLDASNNQISDLEELlDLLSSWPSLRELDLTGNPVCKKPKYRDKIILASKSLEVLDG 202
LRR_8 pfam13855
Leucine rich repeat;
88-146 1.55e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.36  E-value: 1.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 62857821    88 PNLTHLNLSGNRIKDLSTiEPLKKLEHLKSLDLFNcevTNLNDYRENVFKLLPQLTYLD 146
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDD-GAFKGLSNLKVLDLSN---NLLTTLSPGAFSGLPSLRYLD 55
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
88-133 1.77e-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: 41.08  E-value: 1.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 62857821    88 PNLTHLNLSGNRIKDlstIEPLKKLEHLKSLDL-FNCEVTNLNDYRE 133
Cdd:pfam12799   1 PNLEVLDLSNNQITD---IPPLAKLPNLETLDLsGNNKITDLSDLAN 44
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
71-146 2.55e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.54  E-value: 2.55e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62857821  71 LSDNNISGGLEVLAeKCPNLTHLNLSGNRIKDLSTiepLKKLEHLKSLDLFNCEVTNLNDYREnvfklLPQLTYLD 146
Cdd:COG4886 212 LSGNQLTDLPEPLA-NLTNLETLDLSNNQLTDLPE---LGNLTNLEELDLSNNQLTDLPPLAN-----LTNLKTLD 278
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
71-146 5.93e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.77  E-value: 5.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62857821  71 LSDNNISGgLEVLAeKCPNLTHLNLSGNRIKDLStiePLKKLEHLKSLDLFNCEVTNLNDYRENVFKLLPQLTYLD 146
Cdd:COG4886 235 LSNNQLTD-LPELG-NLTNLEELDLSNNQLTDLP---PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLL 305
FBXL18_LRR pfam19729
F-box/LRR-repeat protein 18, LRR; This entry represents the leucine-rich repeats (LRR) from ...
47-128 7.79e-05

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: 43.19  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62857821    47 LSTINVCLSSianlpklnKLKKLELSDNNISGGLEVLAEKCPNLTHLNLSG-------NRIKDLSTIepLKKLEHLKSLD 119
Cdd:pfam19729 267 LSGCVHCLLP--------DSLLRKAEDDIDSSIVETLVACCPNLRHLNLSAahhhsseGLGGHLCAL--LARLKHLRSLS 336

                  ....*....
gi 62857821   120 LFNCEVTNL 128
Cdd:pfam19729 337 LPVCAVADS 345
AMN1 cd09293
Antagonist of mitotic exit network protein 1; Amn1 has been functionally characterized in ...
75-126 2.00e-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: 38.46  E-value: 2.00e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 62857821  75 NIS-GGLEVLAEKCPNLTHLNL----SGNRIKDLSTIEPLKKLEHLKSLDLFNCEVT 126
Cdd:cd09293  90 NITdSGIVALATNCPKLQTINLgrhrNGHLITDVSLSALGKNCTFLQTVGFAGCDVT 146
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
71-123 2.24e-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: 38.23  E-value: 2.24e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 62857821  71 LSDNNISGgLEVLaEKCPNLTHLNLSGNRIkdlSTIEPLKKLEHLKSLDL-FNC 123
Cdd:cd21340  31 LYDNKITK-IENL-EFLTNLTHLYLQNNQI---EKIENLENLVNLKKLYLgGNR 79
 
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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