NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564348041|ref|XP_006237034|]
View 

leiomodin-3 [Rattus norvegicus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1903313)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 3.81e-13

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: 66.93  E-value: 3.81e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041   16 EELDEDEILANLSPEELKELQSEMEVMAPD-PHLPVGMIQKDQTDKAPTGNFDHKSLVDY 74
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHH 68
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 253-392 1.10e-08

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: 57.49  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041 253 SGNQTDLDG--SLRRVRQNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKSFSLANVGADESVAFALANMLRENRSI 330
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564348041 331 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEISRLLKANNTLLKMG 392
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 3.81e-13

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: 66.93  E-value: 3.81e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041   16 EELDEDEILANLSPEELKELQSEMEVMAPD-PHLPVGMIQKDQTDKAPTGNFDHKSLVDY 74
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHH 68
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 253-392 1.10e-08

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: 57.49  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041 253 SGNQTDLDG--SLRRVRQNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKSFSLANVGADESVAFALANMLRENRSI 330
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564348041 331 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEISRLLKANNTLLKMG 392
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 267-361 7.83e-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: 38.88  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041 267 RQNDPDMKELNL--NNIENIPKEMLLdfvNAMKKNKHIKSFSLANVGADESVAFALANMLRENRSITTLNIESNFITGKG 344
Cdd:cd00116  133 KDLPPALEKLVLgrNRLEGASCEALA---KALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEG 209

                         90
                 ....*....|....*..
gi 564348041 345 IVAIMRCLQFNETLTEL 361
Cdd:cd00116  210 ASALAETLASLKSLEVL 226
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 16-74 3.81e-13

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: 66.93  E-value: 3.81e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041   16 EELDEDEILANLSPEELKELQSEMEVMAPD-PHLPVGMIQKDQTDKAPTGNFDHKSLVDY 74
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHH 68
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 253-392 1.10e-08

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: 57.49  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041 253 SGNQTDLDG--SLRRVRQNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKSFSLANVGADESVAFALANMLRENRSI 330
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564348041 331 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEISRLLKANNTLLKMG 392
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 253-361 1.50e-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: 54.03  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041 253 SGNQTDLDG--SLRRVRQNDPDMKELNLNNIeNIPKEMLLDFVNAMKKNKHIKSFSLANVGADESVAFALANMLRENRSI 330
Cdd:COG5238  272 SGNQIGAEGaiALAKALQGNTTLTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                         90       100       110
                 ....*....|....*....|....*....|.
gi 564348041 331 TTLNIESNFITGKGIVAIMRCLQFNETLTEL 361
Cdd:COG5238  351 HSLDLSDNQIGDEGAIALAKYLEGNTTLREL 381
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 267-361 7.83e-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: 38.88  E-value: 7.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564348041 267 RQNDPDMKELNL--NNIENIPKEMLLdfvNAMKKNKHIKSFSLANVGADESVAFALANMLRENRSITTLNIESNFITGKG 344
Cdd:cd00116  133 KDLPPALEKLVLgrNRLEGASCEALA---KALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEG 209

                         90
                 ....*....|....*..
gi 564348041 345 IVAIMRCLQFNETLTEL 361
Cdd:cd00116  210 ASALAETLASLKSLEVL 226
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH