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Conserved domains on  [gi|607344297|ref|NP_001093322|]
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PRAME family member 20 [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 ...
266-391 2.32e-08

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 cd21340:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 220  Bit Score: 54.41  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 266 LRCLQKLYM--NSVSFLEGhLDQmLSCLKTsLNI----LAITNCVLLESD-LKHLSKypsigQLKTLDLSGTRLAnfSLV 338
Cdd:cd21340   67 LVNLKKLYLggNRISVVEG-LEN-LTNLEE-LHIenqrLPPGEKLTFDPRsLAALSN-----SLRVLNISGNNID--SLE 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 607344297 339 PLQVLlekvaATLEYLDLDDCGIVDsqVNAILPALSRCFELTTFSFRGNPIST 391
Cdd:cd21340  137 PLAPL-----RNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPVCK 182
 
Name Accession Description Interval E-value
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
266-391 2.32e-08

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: 54.41  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 266 LRCLQKLYM--NSVSFLEGhLDQmLSCLKTsLNI----LAITNCVLLESD-LKHLSKypsigQLKTLDLSGTRLAnfSLV 338
Cdd:cd21340   67 LVNLKKLYLggNRISVVEG-LEN-LTNLEE-LHIenqrLPPGEKLTFDPRsLAALSN-----SLRVLNISGNNID--SLE 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 607344297 339 PLQVLlekvaATLEYLDLDDCGIVDsqVNAILPALSRCFELTTFSFRGNPIST 391
Cdd:cd21340  137 PLAPL-----RNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
221-410 3.24e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 221 LAEFTPYLGQMRNLRKLVLSDIDsryispeqkkefVTQFTTQFLKLRCLQKLYM--NSVSFLEGHLDQMlsclkTSLNIL 298
Cdd:COG4886  125 LTDLPEELANLTNLKELDLSNNQ------------LTDLPEPLGNLTNLKSLDLsnNQLTDLPEELGNL-----TNLKEL 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 299 AITNCVL--LESDLKHLSKypsigqLKTLDLSGTRLANFSLvPLQVLlekvaATLEYLDLDDCGIVDsqvnaiLPALSRC 376
Cdd:COG4886  188 DLSNNQItdLPEPLGNLTN------LEELDLSGNQLTDLPE-PLANL-----TNLETLDLSNNQLTD------LPELGNL 249
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 607344297 377 FELTTFSFRGNPIST-------ATLENLLCHTIRLNNLCLE 410
Cdd:COG4886  250 TNLEELDLSNNQLTDlpplanlTNLKTLDLSNNQLTDLKLK 290
 
Name Accession Description Interval E-value
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
266-391 2.32e-08

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: 54.41  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 266 LRCLQKLYM--NSVSFLEGhLDQmLSCLKTsLNI----LAITNCVLLESD-LKHLSKypsigQLKTLDLSGTRLAnfSLV 338
Cdd:cd21340   67 LVNLKKLYLggNRISVVEG-LEN-LTNLEE-LHIenqrLPPGEKLTFDPRsLAALSN-----SLRVLNISGNNID--SLE 136
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 607344297 339 PLQVLlekvaATLEYLDLDDCGIVDsqVNAILPALSRCFELTTFSFRGNPIST 391
Cdd:cd21340  137 PLAPL-----RNLEQLDASNNQISD--LEELLDLLSSWPSLRELDLTGNPVCK 182
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
221-410 3.24e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 49.16  E-value: 3.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 221 LAEFTPYLGQMRNLRKLVLSDIDsryispeqkkefVTQFTTQFLKLRCLQKLYM--NSVSFLEGHLDQMlsclkTSLNIL 298
Cdd:COG4886  125 LTDLPEELANLTNLKELDLSNNQ------------LTDLPEPLGNLTNLKSLDLsnNQLTDLPEELGNL-----TNLKEL 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 299 AITNCVL--LESDLKHLSKypsigqLKTLDLSGTRLANFSLvPLQVLlekvaATLEYLDLDDCGIVDsqvnaiLPALSRC 376
Cdd:COG4886  188 DLSNNQItdLPEPLGNLTN------LEELDLSGNQLTDLPE-PLANL-----TNLETLDLSNNQLTD------LPELGNL 249
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 607344297 377 FELTTFSFRGNPIST-------ATLENLLCHTIRLNNLCLE 410
Cdd:COG4886  250 TNLEELDLSNNQLTDlpplanlTNLKTLDLSNNQLTDLKLK 290
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
182-412 1.75e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 182 CKKLKMLGMLFHNIRNILKTV-NLDCIQEVEVNCNWtlpvLAEFTPYLGQMRNLRKLVLSDIDsryispeqkkefVTQFT 260
Cdd:COG4886  112 LTNLESLDLSGNQLTDLPEELaNLTNLKELDLSNNQ----LTDLPEPLGNLTNLKSLDLSNNQ------------LTDLP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 261 TQFLKLRCLQKLYM--NSVSFLEGHLDQMlsclkTSLNILAITNCVL--LESDLKHLSKypsigqLKTLDLSGTRLAnfS 336
Cdd:COG4886  176 EELGNLTNLKELDLsnNQITDLPEPLGNL-----TNLEELDLSGNQLtdLPEPLANLTN------LETLDLSNNQLT--D 242
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 607344297 337 LVPLQVLlekvaATLEYLDLDDCGIVDsqvnaiLPALSRCFELTTFSFRGNPISTATLENLLCHTIRLNNLCLELY 412
Cdd:COG4886  243 LPELGNL-----TNLEELDLSNNQLTD------LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLL 307
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
311-411 6.99e-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: 42.08  E-value: 6.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 607344297 311 KHLSKYPsigQLKTLDLSGTRLANFSLVPLQVLLEKvAATLEYLDLDDCGIVDSQVNAILPALSRCFELTTFSFRGNPIS 390
Cdd:COG5238  286 KALQGNT---TLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIG 361
                         90       100
                 ....*....|....*....|.
gi 607344297 391 TATLEnLLCHTIRLNNLCLEL 411
Cdd:COG5238  362 DEGAI-ALAKYLEGNTTLREL 381
 
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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