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Conserved domains on  [gi|169808413|ref|NP_082162|]
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serine/threonine-protein kinase 11-interacting protein [Mus musculus]

Protein Classification

ATP-binding protein; disease resistance protein; TIR-NBS-LRR class disease resistance protein; leucine-rich repeat domain-containing protein; leucine-rich repeat domain-containing protein; InlB B-repeat-containing protein; leucine-rich repeat domain-containing protein; TIR-NBS-LRR class disease resistance protein; leucine-rich repeat domain-containing protein; leucine-rich repeat domain-containing protein; TIR-NBS-LRR class disease resistance protein; TIR-NBS-LRR class disease resistance protein; TIR-NBS-LRR class disease resistance protein; leucine-rich repeat domain-containing protein; leucine-rich repeat domain-containing protein; TIR-NBS-LRR class disease resistance protein; leucine-rich repeat domain-containing protein; leucine-rich repeat domain-containing protein; leucine-rich repeat-containing serine/threonine-protein kinase; leucine-rich repeat domain-containing protein( domain architecture ID 11723479)

ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain, similar to Saccharomyces cerevisiae checkpoint protein RAD24 and Arabidopsis thaliana disease resistance protein RPS5; ATP-binding protein with an AAA (ATPases Associated with various cellular Activities) domain, similar to magnesium-chelatase subunit ChlI and RuvB-like helicase 1; disease resistance protein contains an N-terminal NB-ARC (also termed nucleotide-binding site, NBS) domain, which is a motif shared by plant and animal proteins whose activation results in cell death; also contains C-terminal leucine-rich repeat (LRR) motifs; TIR (toll/interleukin-1 receptor)-NBS (nucleotide binding site)-LRR (leucine-rich repeat) class disease resistance protein such as Arabidopsis thaliana SNC1 from and Vitis rotundifolia RPV1; resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Caenorhabditis elegans acidic leucine-rich nuclear phosphoprotein 32-related protein 2; InlB B-repeat-containing protein similar to Listeria monocytogenes invasion protein Internalin B (InlB); leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; TIR (toll/interleukin-1 receptor)-NBS (nucleotide binding site)-LRR (leucine-rich repeat) class disease resistance protein such as Arabidopsis thaliana SNC1 from and Vitis rotundifolia RPV1; resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; TIR (toll/interleukin-1 receptor)-NBS (nucleotide binding site)-LRR (leucine-rich repeat) class disease resistance protein such as Arabidopsis thaliana SNC1 from and Vitis rotundifolia RPV1; resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction; TIR (toll/interleukin-1 receptor)-NBS (nucleotide binding site)-LRR (leucine-rich repeat) class disease resistance protein such as Arabidopsis thaliana SNC1 from and Vitis rotundifolia RPV1; resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction; TIR (toll/interleukin-1 receptor)-NBS (nucleotide binding site)-LRR (leucine-rich repeat) class disease resistance protein such as Arabidopsis thaliana SNC1 from and Vitis rotundifolia RPV1; resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; TIR (toll/interleukin-1 receptor)-NBS (nucleotide binding site)-LRR (leucine-rich repeat) class disease resistance protein such as Arabidopsis thaliana SNC1 from and Vitis rotundifolia RPV1; resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Caenorhabditis elegans acidic leucine-rich nuclear phosphoprotein 32-related protein 2; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Homo sapiens leucine-rich repeat-containing protein 1 that may form a complex with DLG1 and ERBIN, where interaction between LRRC1 and ERBIN is indirect; leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions; similar to Homo sapiens lumican that binds to laminin; leucine-rich repeat (LRR)-containing serine/threonine-protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; 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
LIP1 super family cl24471
LKB1 serine/threonine kinase interacting protein 1; LIP1 is a protein found in eukaryotes. It ...
 4-94 5.54e-32

LKB1 serine/threonine kinase interacting protein 1; LIP1 is a protein found in eukaryotes. It represents the N-terminus of a leucine-rich-repeat protein that is implicated in Peutz-Jeghers syndrome. LIP1 interacts with the TGF-beta-regulated transcription factor SMAD4 to form a LKB1-LIP1-SMAD4 ternary complex. Mutations in SMAD4 lead to juvenile polyposis, suggesting a mechanistic link between these two diseases.


The actual alignment was detected with superfamily member pfam15904:

Pssm-ID: 464931  Cd Length: 90  Bit Score: 119.90  E-value: 5.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413     4 APRDSVVWKLAGLLRESGDAVLSGCSTLSLLTATLQQLNRVFELYLGPWGPgQTGFVALPSHPADSPVILQLQFLFDVLQ 83
Cdd:pfam15904    1 SDPEPLVHSLANLLRNNGDLVLDGSSTLTLSASSLQHLTRSFEQHLLPRSH-QHGFLALPSHPADTSSLLQLQFLFDMLQ 79

                           90
                   ....*....|.
gi 169808413    84 KTLSLKLVHIP 94
Cdd:pfam15904   80 KTTSLKLIHVP 90
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
89-291 3.21e-13

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.04  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413   89 KLVHIPGVGLPGPIKIFPFKSLRQLELRGVPIHSLCGLRGIYSQLESLVCNRSiqALEELLSACGGdlCSALPWLallsa 168
Cdd:COG4886    94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNN--QLTDLPEPLGN--LTNLKSL----- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  169 DFSYNALRSLDSSLRLLSALRFLNLSHNHLQDCKGFLMDLCELYHLDISYNHLRLVPRVGPSGAALGTLILRANELRSLQ 248
Cdd:COG4886   165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 169808413  249 GLEQLKNLRHLDVAYNLLeghTELAPLWLLAELRKLYLEGNPL 291
Cdd:COG4886   245 ELGNLTNLEELDLSNNQL---TDLPPLANLTNLKTLDLSNNQL 284
 
Name Accession Description Interval E-value
LIP1 pfam15904
LKB1 serine/threonine kinase interacting protein 1; LIP1 is a protein found in eukaryotes. It ...
 4-94 5.54e-32

LKB1 serine/threonine kinase interacting protein 1; LIP1 is a protein found in eukaryotes. It represents the N-terminus of a leucine-rich-repeat protein that is implicated in Peutz-Jeghers syndrome. LIP1 interacts with the TGF-beta-regulated transcription factor SMAD4 to form a LKB1-LIP1-SMAD4 ternary complex. Mutations in SMAD4 lead to juvenile polyposis, suggesting a mechanistic link between these two diseases.


Pssm-ID: 464931  Cd Length: 90  Bit Score: 119.90  E-value: 5.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413     4 APRDSVVWKLAGLLRESGDAVLSGCSTLSLLTATLQQLNRVFELYLGPWGPgQTGFVALPSHPADSPVILQLQFLFDVLQ 83
Cdd:pfam15904    1 SDPEPLVHSLANLLRNNGDLVLDGSSTLTLSASSLQHLTRSFEQHLLPRSH-QHGFLALPSHPADTSSLLQLQFLFDMLQ 79

                           90
                   ....*....|.
gi 169808413    84 KTLSLKLVHIP 94
Cdd:pfam15904   80 KTTSLKLIHVP 90
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
89-291 3.21e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.04  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413   89 KLVHIPGVGLPGPIKIFPFKSLRQLELRGVPIHSLCGLRGIYSQLESLVCNRSiqALEELLSACGGdlCSALPWLallsa 168
Cdd:COG4886    94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNN--QLTDLPEPLGN--LTNLKSL----- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  169 DFSYNALRSLDSSLRLLSALRFLNLSHNHLQDCKGFLMDLCELYHLDISYNHLRLVPRVGPSGAALGTLILRANELRSLQ 248
Cdd:COG4886   165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 169808413  249 GLEQLKNLRHLDVAYNLLeghTELAPLWLLAELRKLYLEGNPL 291
Cdd:COG4886   245 ELGNLTNLEELDLSNNQL---TDLPPLANLTNLKTLDLSNNQL 284
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 191-321 1.36e-07

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: 53.25  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  191 LNLSHNHLQDCKGfLMDLCELYHLDISYNHL----------RLVPRVGPSgaaLGTLILRANELRSLQGLEQLKNLRHLD 260
Cdd:cd21340    73 LYLGGNRISVVEG-LENLTNLEELHIENQRLppgekltfdpRSLAALSNS---LRVLNISGNNIDSLEPLAPLRNLEQLD 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169808413  261 VAYNLLEGHTELAPLWL-LAELRKLYLEGNPLwfhpahrAATAQYlspraRD---AAHGFL--LDGK 321
Cdd:cd21340   149 ASNNQISDLEELLDLLSsWPSLRELDLTGNPV-------CKKPKY-----RDkiiLASKSLevLDGK 203
LRR_8 pfam13855
Leucine rich repeat;
236-291 1.12e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 1.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413   236 TLILRANELRSLQG--LEQLKNLRHLDVAYNLLeghTELAP--LWLLAELRKLYLEGNPL 291
Cdd:pfam13855    5 SLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLL---TTLSPgaFSGLPSLRYLDLSGNRL 61
 
Name Accession Description Interval E-value
LIP1 pfam15904
LKB1 serine/threonine kinase interacting protein 1; LIP1 is a protein found in eukaryotes. It ...
 4-94 5.54e-32

LKB1 serine/threonine kinase interacting protein 1; LIP1 is a protein found in eukaryotes. It represents the N-terminus of a leucine-rich-repeat protein that is implicated in Peutz-Jeghers syndrome. LIP1 interacts with the TGF-beta-regulated transcription factor SMAD4 to form a LKB1-LIP1-SMAD4 ternary complex. Mutations in SMAD4 lead to juvenile polyposis, suggesting a mechanistic link between these two diseases.


Pssm-ID: 464931  Cd Length: 90  Bit Score: 119.90  E-value: 5.54e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413     4 APRDSVVWKLAGLLRESGDAVLSGCSTLSLLTATLQQLNRVFELYLGPWGPgQTGFVALPSHPADSPVILQLQFLFDVLQ 83
Cdd:pfam15904    1 SDPEPLVHSLANLLRNNGDLVLDGSSTLTLSASSLQHLTRSFEQHLLPRSH-QHGFLALPSHPADTSSLLQLQFLFDMLQ 79

                           90
                   ....*....|.
gi 169808413    84 KTLSLKLVHIP 94
Cdd:pfam15904   80 KTTSLKLIHVP 90
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
89-291 3.21e-13

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 73.04  E-value: 3.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413   89 KLVHIPGVGLPGPIKIFPFKSLRQLELRGVPIHSLCGLRGIYSQLESLVCNRSiqALEELLSACGGdlCSALPWLallsa 168
Cdd:COG4886    94 DLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNN--QLTDLPEPLGN--LTNLKSL----- 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  169 DFSYNALRSLDSSLRLLSALRFLNLSHNHLQDCKGFLMDLCELYHLDISYNHLRLVPRVGPSGAALGTLILRANELRSLQ 248
Cdd:COG4886   165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 169808413  249 GLEQLKNLRHLDVAYNLLeghTELAPLWLLAELRKLYLEGNPL 291
Cdd:COG4886   245 ELGNLTNLEELDLSNNQL---TDLPPLANLTNLKTLDLSNNQL 284
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
101-291 7.62e-08

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 56.10  E-value: 7.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  101 PIKIFPFKSLRQLELRGVPIHSLC-GLRGIySQLESLVCNR-SIQALEELLSACggdlcSALPWLallsaDFSYNALRSL 178
Cdd:COG4886   129 PEELANLTNLKELDLSNNQLTDLPePLGNL-TNLKSLDLSNnQLTDLPEELGNL-----TNLKEL-----DLSNNQITDL 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  179 DSSLRLLSALRFLNLSHNHLQDCKGFLMDLCELYHLDISYNHLRLVPRVGpSGAALGTLILRANELRSLQGLEQLKNLRH 258
Cdd:COG4886   198 PEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLPELG-NLTNLEELDLSNNQLTDLPPLANLTNLKT 276

                         170       180       190
                  ....*....|....*....|....*....|...
gi 169808413  259 LDVAYNLLEGhTELAPLWLLAELRKLYLEGNPL 291
Cdd:COG4886   277 LDLSNNQLTD-LKLKELELLLGLNSLLLLLLLL 308
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 191-321 1.36e-07

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: 53.25  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413  191 LNLSHNHLQDCKGfLMDLCELYHLDISYNHL----------RLVPRVGPSgaaLGTLILRANELRSLQGLEQLKNLRHLD 260
Cdd:cd21340    73 LYLGGNRISVVEG-LENLTNLEELHIENQRLppgekltfdpRSLAALSNS---LRVLNISGNNIDSLEPLAPLRNLEQLD 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169808413  261 VAYNLLEGHTELAPLWL-LAELRKLYLEGNPLwfhpahrAATAQYlspraRD---AAHGFL--LDGK 321
Cdd:cd21340   149 ASNNQISDLEELLDLLSsWPSLRELDLTGNPV-------CKKPKY-----RDkiiLASKSLevLDGK 203
LRR_8 pfam13855
Leucine rich repeat;
236-291 1.12e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 1.12e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169808413   236 TLILRANELRSLQG--LEQLKNLRHLDVAYNLLeghTELAP--LWLLAELRKLYLEGNPL 291
Cdd:pfam13855    5 SLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLL---TTLSPgaFSGLPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 236-289 5.00e-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: 42.85  E-value: 5.00e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 169808413  236 TLILRANELRSLQGLEQLKNLRHLDVAYNLLEghtELAPLWLLAELRKLYLEGN 289
Cdd:cd21340    28 VLYLYDNKITKIENLEFLTNLTHLYLQNNQIE---KIENLENLVNLKKLYLGGN 78
LRR_8 pfam13855
Leucine rich repeat;
191-266 6.69e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 35.96  E-value: 6.69e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169808413   191 LNLSHNHLQD-CKGFLMDLCELYHLDISYNHLRLVprvgpsgaalgtlilranelrSLQGLEQLKNLRHLDVAYNLL 266
Cdd:pfam13855    6 LDLSNNRLTSlDDGAFKGLSNLKVLDLSNNLLTTL---------------------SPGAFSGLPSLRYLDLSGNRL 61
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 234-264 9.41e-03

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: 35.30  E-value: 9.41e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 169808413   234 LGTLILRANELRSLQGLEQLKNLRHLDVAYN 264
Cdd:pfam12799    3 LEVLDLSNNQITDIPPLAKLPNLETLDLSGN 33
 
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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