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Conserved domains on  [gi|1228981453|ref|XP_022054812|]
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leucine-rich repeat-containing protein 42 isoform X1 [Acanthochromis polyacanthus]

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];
144-248 1.51e-05

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: 46.85  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 144 DAIKTFHSLKSLDLFGCKLGDNHELFQHLTstslasSLIELFIGGNSLSDaglqrLTAPIrmmrKGLDCLQLLDLSYNPI 223
Cdd:COG4886   130 EELANLTNLKELDLSNNQLTDLPEPLGNLT------NLKSLDLSNNQLTD-----LPEEL----GNLTNLKELDLSNNQI 194
                          90       100
                  ....*....|....*....|....*
gi 1228981453 224 SEAALRyLTCFPKLVKLDLSGTSLK 248
Cdd:COG4886   195 TDLPEP-LGNLTNLEELDLSGNQLT 218
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
144-248 1.51e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 144 DAIKTFHSLKSLDLFGCKLGDNHELFQHLTstslasSLIELFIGGNSLSDaglqrLTAPIrmmrKGLDCLQLLDLSYNPI 223
Cdd:COG4886   130 EELANLTNLKELDLSNNQLTDLPEPLGNLT------NLKSLDLSNNQLTD-----LPEEL----GNLTNLKELDLSNNQI 194
                          90       100
                  ....*....|....*....|....*
gi 1228981453 224 SEAALRyLTCFPKLVKLDLSGTSLK 248
Cdd:COG4886   195 TDLPEP-LGNLTNLEELDLSGNQLT 218
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
145-250 6.57e-05

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: 44.65  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 145 AIKTFHSLKSLDLFGCKLGD-NHELFQHLTSTSlaSSLIELFIGGNSLSDAGLQRLtAPIrmMRKGLDCLQLLDLSYNPI 223
Cdd:cd00116   188 GLKANCNLEVLDLNNNGLTDeGASALAETLASL--KSLEVLNLGDNNLTDAGAAAL-ASA--LLSPNISLLTLSLSCNDI 262
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1228981453 224 ----SEAALRYLTCFPKLVKLDLSGTSLKLE 250
Cdd:cd00116   263 tddgAKDLAEVLAEKESLLELDLRGNKFGEE 293
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
144-248 1.51e-05

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 46.85  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 144 DAIKTFHSLKSLDLFGCKLGDNHELFQHLTstslasSLIELFIGGNSLSDaglqrLTAPIrmmrKGLDCLQLLDLSYNPI 223
Cdd:COG4886   130 EELANLTNLKELDLSNNQLTDLPEPLGNLT------NLKSLDLSNNQLTD-----LPEEL----GNLTNLKELDLSNNQI 194
                          90       100
                  ....*....|....*....|....*
gi 1228981453 224 SEAALRyLTCFPKLVKLDLSGTSLK 248
Cdd:COG4886   195 TDLPEP-LGNLTNLEELDLSGNQLT 218
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
145-250 6.57e-05

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: 44.65  E-value: 6.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 145 AIKTFHSLKSLDLFGCKLGD-NHELFQHLTSTSlaSSLIELFIGGNSLSDAGLQRLtAPIrmMRKGLDCLQLLDLSYNPI 223
Cdd:cd00116   188 GLKANCNLEVLDLNNNGLTDeGASALAETLASL--KSLEVLNLGDNNLTDAGAAAL-ASA--LLSPNISLLTLSLSCNDI 262
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1228981453 224 ----SEAALRYLTCFPKLVKLDLSGTSLKLE 250
Cdd:cd00116   263 tddgAKDLAEVLAEKESLLELDLRGNKFGEE 293
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
137-247 1.31e-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: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 137 PLLQERMDAIKTFHSLKSLDLFGCKLGDNHELFQHLTSTSLASSLIELFIGGNSLSDAGLQRLTAPIRMMRKgldcLQLL 216
Cdd:cd00116    95 PDGCGVLESLLRSSSLQELKLNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANRD----LKEL 170
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1228981453 217 DLSYNPISEAALRYL----TCFPKLVKLDLSGTSL 247
Cdd:cd00116   171 NLANNGIGDAGIRALaeglKANCNLEVLDLNNNGL 205
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
144-248 2.28e-04

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 2.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 144 DAIKTFHSLKSLDLFGCKLGDNHELFQHLTStslassLIELFIGGNSLSDaglqrLTAPIRMMRKgldcLQLLDLSYNPI 223
Cdd:COG4886   153 EPLGNLTNLKSLDLSNNQLTDLPEELGNLTN------LKELDLSNNQITD-----LPEPLGNLTN----LEELDLSGNQL 217
                          90       100
                  ....*....|....*....|....*..
gi 1228981453 224 SE--AALRYLTcfpKLVKLDLSGTSLK 248
Cdd:COG4886   218 TDlpEPLANLT---NLETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
144-264 1.49e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 40.69  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 144 DAIKTFHSLKSLDLFGCKLGDNHELFQhltstslASSLIELFIGGNSLSDAGLQrltapirmmrKGLDCLQLLDLSYNPI 223
Cdd:COG4886   222 EPLANLTNLETLDLSNNQLTDLPELGN-------LTNLEELDLSNNQLTDLPPL----------ANLTNLKTLDLSNNQL 284
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1228981453 224 SEAALRYLTCFPKLVKLDLSGTSLKLETGLKTTILKLLGLI 264
Cdd:COG4886   285 TDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLL 325
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
145-226 2.33e-03

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: 39.77  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228981453 145 AIKTFHSLKSLDLFGCKLGDN--HELFQHLTSTslaSSLIELFIGGNSLSDAGLQRLTApirmMRKGLDCLQLLDLSYNP 222
Cdd:COG5238   231 ALKGNKSLTTLDLSNNQIGDEgvIALAEALKNN---TTVETLYLSGNQIGAEGAIALAK----ALQGNTTLTSLDLSVNR 303

                  ....
gi 1228981453 223 ISEA 226
Cdd:COG5238   304 IGDE 307
 
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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