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Conserved domains on  [gi|1950408351|ref|XP_038244680|]
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leucine-rich repeat-containing protein 14 isoform X4 [Dermochelys coriacea]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1001123)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Oryctolagus cuniculus monocyte differentiation antigen CD14, a coreceptor for bacterial lipopolysaccharide

Gene Ontology:  GO:0005515
PubMed:  11751054

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
243-431 4.51e-08

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


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 243 DLRFNNLGLSGLRVILPHMAKFTNLVSLKLPYSNIdvrrlsagmegslHYFATQLSRLSCLKELNLGSSRLSGkLKQLLG 322
Cdd:COG4886   114 NLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------------TDLPEPLGNLTNLKSLDLSNNQLTD-LPEELG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 323 DLQGpLESLELAFCYL--LPNDLAYLSQslhtptLKKLDLSGNNLSeSLLQPFQHLleeasSSLLHLDIMECRLMDI--- 397
Cdd:COG4886   180 NLTN-LKELDLSNNQItdLPEPLGNLTN------LEELDLSGNQLT-DLPEPLANL-----TNLETLDLSNNQLTDLpel 246
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1950408351 398 ----HLELL---------LPALCRCSQLRYLGVFGNPLFTRGLKNLL 431
Cdd:COG4886   247 gnltNLEELdlsnnqltdLPPLANLTNLKTLDLSNNQLTDLKLKELE 293
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
243-431 4.51e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 243 DLRFNNLGLSGLRVILPHMAKFTNLVSLKLPYSNIdvrrlsagmegslHYFATQLSRLSCLKELNLGSSRLSGkLKQLLG 322
Cdd:COG4886   114 NLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------------TDLPEPLGNLTNLKSLDLSNNQLTD-LPEELG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 323 DLQGpLESLELAFCYL--LPNDLAYLSQslhtptLKKLDLSGNNLSeSLLQPFQHLleeasSSLLHLDIMECRLMDI--- 397
Cdd:COG4886   180 NLTN-LKELDLSNNQItdLPEPLGNLTN------LEELDLSGNQLT-DLPEPLANL-----TNLETLDLSNNQLTDLpel 246
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1950408351 398 ----HLELL---------LPALCRCSQLRYLGVFGNPLFTRGLKNLL 431
Cdd:COG4886   247 gnltNLEELdlsnnqltdLPPLANLTNLKTLDLSNNQLTDLKLKELE 293
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
297-422 1.14e-05

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: 46.70  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 297 LSRLSCLKELNLGS---SRLSG-----KLKQLLGDLQGPLESLELAFcylLPNDLAYLSQSLHTptlkkLDLSGNNLSEs 368
Cdd:cd21340    64 LENLVNLKKLYLGGnriSVVEGlenltNLEELHIENQRLPPGEKLTF---DPRSLAALSNSLRV-----LNISGNNIDS- 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950408351 369 lLQPFQHLleeasSSLLHLDIMECRLMDIhlELLLPALCRCSQLRYLGVFGNPL 422
Cdd:cd21340   135 -LEPLAPL-----RNLEQLDASNNQISDL--EELLDLLSSWPSLRELDLTGNPV 180
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
243-431 4.51e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 55.32  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 243 DLRFNNLGLSGLRVILPHMAKFTNLVSLKLPYSNIdvrrlsagmegslHYFATQLSRLSCLKELNLGSSRLSGkLKQLLG 322
Cdd:COG4886   114 NLESLDLSGNQLTDLPEELANLTNLKELDLSNNQL-------------TDLPEPLGNLTNLKSLDLSNNQLTD-LPEELG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 323 DLQGpLESLELAFCYL--LPNDLAYLSQslhtptLKKLDLSGNNLSeSLLQPFQHLleeasSSLLHLDIMECRLMDI--- 397
Cdd:COG4886   180 NLTN-LKELDLSNNQItdLPEPLGNLTN------LEELDLSGNQLT-DLPEPLANL-----TNLETLDLSNNQLTDLpel 246
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1950408351 398 ----HLELL---------LPALCRCSQLRYLGVFGNPLFTRGLKNLL 431
Cdd:COG4886   247 gnltNLEELdlsnnqltdLPPLANLTNLKTLDLSNNQLTDLKLKELE 293
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
297-422 1.14e-05

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: 46.70  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 297 LSRLSCLKELNLGS---SRLSG-----KLKQLLGDLQGPLESLELAFcylLPNDLAYLSQSLHTptlkkLDLSGNNLSEs 368
Cdd:cd21340    64 LENLVNLKKLYLGGnriSVVEGlenltNLEELHIENQRLPPGEKLTF---DPRSLAALSNSLRV-----LNISGNNIDS- 134
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1950408351 369 lLQPFQHLleeasSSLLHLDIMECRLMDIhlELLLPALCRCSQLRYLGVFGNPL 422
Cdd:cd21340   135 -LEPLAPL-----RNLEQLDASNNQISDL--EELLDLLSSWPSLRELDLTGNPV 180
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
197-442 1.32e-05

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: 47.48  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 197 VLKDALQNNANSMLRLKCRdfraeelpIASTVGLL--EFLDPTGVRQVDLRFNNLGLSGLRVILPHMAKFTNLVSLKLPY 274
Cdd:COG5238   146 VLKDPLGGNAVHLLGLAAR--------LGLLAAISmaKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKR 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 275 SNIDVRrlsaGMEGslhyFATQLSRLSCLKELNLGSSRLSGKLKQLLGD-LQGP--LESLELAFCYLLPNDLAYLSQSLH 351
Cdd:COG5238   218 NPIGDE----GAEI----LAEALKGNKSLTTLDLSNNQIGDEGVIALAEaLKNNttVETLYLSGNQIGAEGAIALAKALQ 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 352 T-PTLKKLDLSGNNLSESLLQPFQHLLEEaSSSLLHLDIMECRLMDIHLELLLPALCRCSQLRYLGVFGNPLFTRG---L 427
Cdd:COG5238   290 GnTTLTSLDLSVNRIGDEGAIALAEGLQG-NKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGaiaL 368
                         250
                  ....*....|....*
gi 1950408351 428 KNLLQKTMGLLYLQL 442
Cdd:COG5238   369 AKYLEGNTTLRELNL 383
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
197-432 2.22e-05

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: 46.71  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 197 VLKDAL-QNNANSMLRLKcrdfraeELPIA--STVGLLEFL-DPTGVRQVDLRFNNLGLSGLRVILPHMAKFTNLVSLKL 272
Cdd:COG5238   199 ELAEALtQNTTVTTLWLK-------RNPIGdeGAEILAEALkGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYL 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 273 PYSNIDVrrlsAGMEGslhyFATQLSRLSCLKELNLGSSRLSGklkqllgdlQGPLEslelafcyllpndlayLSQSL-H 351
Cdd:COG5238   272 SGNQIGA----EGAIA----LAKALQGNTTLTSLDLSVNRIGD---------EGAIA----------------LAEGLqG 318
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 352 TPTLKKLDLSGNNLSESLLQP-FQHLleEASSSLLHLDIMECRLMDIHLELLLPALCRCSQLRYLGVFGNPLFTRGLKNL 430
Cdd:COG5238   319 NKTLHTLNLAYNGIGAQGAIAlAKAL--QENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAL 396

                  ..
gi 1950408351 431 LQ 432
Cdd:COG5238   397 ID 398
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
198-384 4.82e-05

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: 45.94  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 198 LKDALQNNAN-SMLRLKCRDFRAEELpiastVGLLEFL-DPTGVRQVDLRFNNLGLSGLRVILPHMAKFTNLVSLKLPYS 275
Cdd:COG5238   256 LAEALKNNTTvETLYLSGNQIGAEGA-----IALAKALqGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 276 NIDVrrlsAGMEGslhyFATQLSRLSCLKELNLGSSRLSGK----LKQLLGDLQGpLESLELAFCYLLPNDLAYLSQSLH 351
Cdd:COG5238   331 GIGA----QGAIA----LAKALQENTTLHSLDLSDNQIGDEgaiaLAKYLEGNTT-LRELNLGKNNIGKQGAEALIDALQ 401
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1950408351 352 TPTLKKLDLSGNNLSESLLQPFQHLLEEASSSL 384
Cdd:COG5238   402 TNRLHTLILDGNLIGAEAQQRLEQLLERIKSVY 434
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
240-392 1.95e-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: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1950408351 240 RQVDLRFNNLGLSGLRVILPHMAKFTNLVSLKLpySNIDVRRLSAGMegslhyFATQLSRLSCLKELNLGSSRLSGK--- 316
Cdd:cd00116   168 KELNLANNGIGDAGIRALAEGLKANCNLEVLDL--NNNGLTDEGASA------LAETLASLKSLEVLNLGDNNLTDAgaa 239
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1950408351 317 --LKQLLGDLQGpLESLELAFCYLLPNDLAYLSQSL-HTPTLKKLDLSGNNLSESLLQPFQHLLEEASSSLLHLDIMEC 392
Cdd:cd00116   240 alASALLSPNIS-LLTLSLSCNDITDDGAKDLAEVLaEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESLWVKDD 317
 
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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