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Conserved domains on  [gi|568942172|ref|XP_006506334|]
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leiomodin-3 isoform X1 [Mus musculus]

Protein Classification

Tropomodulin and PPP1R42 superfamily-containing protein( domain architecture ID 1903313)

Tropomodulin and PPP1R42 superfamily-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomodulin super family cl12276
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 16-74 1.23e-12

Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of erythrocyte tropomyosin and blocks head-to-tail association of tropomyosin along actin filaments. Limited proteolysis shows this protein is composed of two domains. The amino terminal domain contains the tropomyosin binding function.


The actual alignment was detected with superfamily member pfam03250:

Pssm-ID: 460862  Cd Length: 142  Bit Score: 65.38  E-value: 1.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172   16 EELDEDELLANLSPEELKELQSEMEVMAPD-PHLPVGMIQKDQTDKAPTGNFNHKSLVDY 74
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHH 68
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 246-385 7.77e-09

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 57.88  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 246 SGNQTDLDG--SLRRVRQNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSV 323
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568942172 324 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEISRLLKANTTLLKMG 385
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 16-74 1.23e-12

Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of erythrocyte tropomyosin and blocks head-to-tail association of tropomyosin along actin filaments. Limited proteolysis shows this protein is composed of two domains. The amino terminal domain contains the tropomyosin binding function.


Pssm-ID: 460862  Cd Length: 142  Bit Score: 65.38  E-value: 1.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172   16 EELDEDELLANLSPEELKELQSEMEVMAPD-PHLPVGMIQKDQTDKAPTGNFNHKSLVDY 74
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHH 68
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 246-385 7.77e-09

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: 57.88  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 246 SGNQTDLDG--SLRRVRQNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSV 323
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568942172 324 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEISRLLKANTTLLKMG 385
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 195-355 1.40e-03

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: 41.19  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 195 NPGTYQQLATKTAHEQ---KDTSETKEKGEKKIAKLDPKKLALDTSFLKVSARPSGNQTDLDGSLRRVRqndpDMKELNL 271
Cdd:cd00116   97 GCGVLESLLRSSSLQElklNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANR----DLKELNL 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 272 -NNieNIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSVTTLNIESNFITGKGIVAImrCLQFNET 350
Cdd:cd00116  173 aNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAAL--ASALLSP 248


                 ....*
gi 568942172 351 LTELR 355
Cdd:cd00116  249 NISLL 253
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 16-74 1.23e-12

Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of erythrocyte tropomyosin and blocks head-to-tail association of tropomyosin along actin filaments. Limited proteolysis shows this protein is composed of two domains. The amino terminal domain contains the tropomyosin binding function.


Pssm-ID: 460862  Cd Length: 142  Bit Score: 65.38  E-value: 1.23e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172   16 EELDEDELLANLSPEELKELQSEMEVMAPD-PHLPVGMIQKDQTDKAPTGNFNHKSLVDY 74
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHH 68
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 246-385 7.77e-09

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: 57.88  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 246 SGNQTDLDG--SLRRVRQNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSV 323
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568942172 324 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEISRLLKANTTLLKMG 385
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 246-354 1.18e-07

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: 54.41  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 246 SGNQTDLDG--SLRRVRQNDPDMKELNLNNIeNIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSV 323
Cdd:COG5238  272 SGNQIGAEGaiALAKALQGNTTLTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                         90       100       110
                 ....*....|....*....|....*....|.
gi 568942172 324 TTLNIESNFITGKGIVAIMRCLQFNETLTEL 354
Cdd:COG5238  351 HSLDLSDNQIGDEGAIALAKYLEGNTTLREL 381
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 195-355 1.40e-03

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: 41.19  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 195 NPGTYQQLATKTAHEQ---KDTSETKEKGEKKIAKLDPKKLALDTSFLKVSARPSGNQTDLDGSLRRVRqndpDMKELNL 271
Cdd:cd00116   97 GCGVLESLLRSSSLQElklNNNGLGDRGLRLLAKGLKDLPPALEKLVLGRNRLEGASCEALAKALRANR----DLKELNL 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 272 -NNieNIPKEMLLDFVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSVTTLNIESNFITGKGIVAImrCLQFNET 350
Cdd:cd00116  173 aNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAAL--ASALLSP 248


                 ....*
gi 568942172 351 LTELR 355
Cdd:cd00116  249 NISLL 253
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 285-381 2.29e-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: 40.54  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568942172 285 FVNAMKKNKHIKTFSLANVGADESVAFALANMLRENRSVTTLNIESNFITGKGIVAIMRCLQFNETLTELRFHNQRhmLG 364
Cdd:COG5238  172 SMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQ--IG 249

                         90
                 ....*....|....*..
gi 568942172 365 HHAEMEISRLLKANTTL 381
Cdd:COG5238  250 DEGVIALAEALKNNTTV 266
 
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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