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Conserved domains on  [gi|118572771|sp|Q0VAK6|]
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RecName: Full=Leiomodin-3; AltName: Full=Leiomodin, fetal form

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

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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 ...
 6-96 7.22e-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: 66.16  E-value: 7.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771    6 RNSDQEELLDeeINEDEILANLSAEELKELQSEMEVMAPDPS-LPVGMIQKDQTDKPPTGNFNHKSLVDYMYwEKASRRM 84
Cdd:pfam03250   1 YKKDLKKYDD--IDEDELLKKLSEEELEQLDELLEELDPDNAlLPAGQRQRDQTKKEPTGPFDREKLLHHLE-KQALEPK 77

                          90
                  ....*....|..
gi 118572771   85 LEEERVPVTFVK 96
Cdd:pfam03250  78 DREDVVPFTGEK 89
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-374 6.90e-10

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: 61.34  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 235 SGNQTDLDG--SLRRVRKNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKTFSLANVGADENVAFALANMLRENRSI 312
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572771 313 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEIARLLKANNTLLKMG 374
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 ...
 6-96 7.22e-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: 66.16  E-value: 7.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771    6 RNSDQEELLDeeINEDEILANLSAEELKELQSEMEVMAPDPS-LPVGMIQKDQTDKPPTGNFNHKSLVDYMYwEKASRRM 84
Cdd:pfam03250   1 YKKDLKKYDD--IDEDELLKKLSEEELEQLDELLEELDPDNAlLPAGQRQRDQTKKEPTGPFDREKLLHHLE-KQALEPK 77

                          90
                  ....*....|..
gi 118572771   85 LEEERVPVTFVK 96
Cdd:pfam03250  78 DREDVVPFTGEK 89
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-374 6.90e-10

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: 61.34  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 235 SGNQTDLDG--SLRRVRKNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKTFSLANVGADENVAFALANMLRENRSI 312
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572771 313 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEIARLLKANNTLLKMG 374
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 253-374 4.06e-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: 39.65  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 253 PDMKELNL-NNieNIPKEMLLDFVNAMKKNKHIKTFSLANVG-ADENVAfALANMLRENRSITTLNIESNFITGKGIVAI 330
Cdd:cd00116  165 RDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGlTDEGAS-ALAETLASLKSLEVLNLGDNNLTDAGAAAL 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 118572771 331 mrCLQF---NETLTELRFHNQRhmLGHHAEMEIARLLKANNTLLKMG 374
Cdd:cd00116  242 --ASALlspNISLLTLSLSCND--ITDDGAKDLAEVLAEKESLLELD 284
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 6-96 7.22e-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: 66.16  E-value: 7.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771    6 RNSDQEELLDeeINEDEILANLSAEELKELQSEMEVMAPDPS-LPVGMIQKDQTDKPPTGNFNHKSLVDYMYwEKASRRM 84
Cdd:pfam03250   1 YKKDLKKYDD--IDEDELLKKLSEEELEQLDELLEELDPDNAlLPAGQRQRDQTKKEPTGPFDREKLLHHLE-KQALEPK 77

                          90
                  ....*....|..
gi 118572771   85 LEEERVPVTFVK 96
Cdd:pfam03250  78 DREDVVPFTGEK 89
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-374 6.90e-10

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: 61.34  E-value: 6.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 235 SGNQTDLDG--SLRRVRKNDPDMKELNLNNiENIPKEMLLDFVNAMKKNKHIKTFSLANVGADENVAFALANMLRENRSI 312
Cdd:COG5238  188 GCNQIGDEGieELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572771 313 TTLNIESNFITGKGIVAIMRCLQFNETLTELRF-HNQrhmLGHHAEMEIARLLKANNTLLKMG 374
Cdd:COG5238  267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 235-392 7.89e-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: 54.80  E-value: 7.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 235 SGNQTDLDG--SLRRVRKNDPDMKELNLNNIeNIPKEMLLDFVNAMKKNKHIKTFSLANVGADENVAFALANMLRENRSI 312
Cdd:COG5238  272 SGNQIGAEGaiALAKALQGNTTLTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTL 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 313 TTLNIESNFITGKGIVAIMRCLQFNETLTELrfHNQRHMLGHHAEMEIARLLKANN-TLLKMGYHFELPGPRMVVTNLLT 391
Cdd:COG5238  351 HSLDLSDNQIGDEGAIALAKYLEGNTTLREL--NLGKNNIGKQGAEALIDALQTNRlHTLILDGNLIGAEAQQRLEQLLE 428


                 .
gi 118572771 392 R 392
Cdd:COG5238  429 R 429
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 274-370 3.10e-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: 40.16  E-value: 3.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 274 FVNAMKKNKHIKTFSLANVGADENVAFALANMLRENRSITTLNIESNFITGKGIVAIMRCLQFNETLTELRFHNQRhmLG 353
Cdd:COG5238  172 SMAKALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQ--IG 249

                         90
                 ....*....|....*..
gi 118572771 354 HHAEMEIARLLKANNTL 370
Cdd:COG5238  250 DEGVIALAEALKNNTTV 266
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 253-374 4.06e-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: 39.65  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572771 253 PDMKELNL-NNieNIPKEMLLDFVNAMKKNKHIKTFSLANVG-ADENVAfALANMLRENRSITTLNIESNFITGKGIVAI 330
Cdd:cd00116  165 RDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGlTDEGAS-ALAETLASLKSLEVLNLGDNNLTDAGAAAL 241

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 118572771 331 mrCLQF---NETLTELRFHNQRhmLGHHAEMEIARLLKANNTLLKMG 374
Cdd:cd00116  242 --ASALlspNISLLTLSLSCND--ITDDGAKDLAEVLAEKESLLELD 284
 
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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