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Conserved domains on  [gi|1958774800|ref|XP_038965242|]
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tropomodulin-1 isoform X1 [Rattus norvegicus]

Protein Classification

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 ...
 6-41 1.05e-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: 66.54  E-value: 1.05e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774800   6 ESVTLEPELEEALANASDAELCDIAAILGMHTLMSN 41
Cdd:pfam03250 107 EAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 81-212 7.09e-11

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: 61.73  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  81 VEETLERIKNNDpELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 160
Cdd:COG5238   253 VIALAEALKNNT-TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958774800 161 FISGAGILCLVEALPHNTSLVELK-IDNQsqpLGNKVEMEIVNMLEKNTTLLK 212
Cdd:COG5238   331 GIGAQGAIALAKALQENTTLHSLDlSDNQ---IGDEGAIALAKYLEGNTTLRE 380
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 6-41 1.05e-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: 66.54  E-value: 1.05e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774800   6 ESVTLEPELEEALANASDAELCDIAAILGMHTLMSN 41
Cdd:pfam03250 107 EAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 81-212 7.09e-11

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: 61.73  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  81 VEETLERIKNNDpELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 160
Cdd:COG5238   253 VIALAEALKNNT-TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958774800 161 FISGAGILCLVEALPHNTSLVELK-IDNQsqpLGNKVEMEIVNMLEKNTTLLK 212
Cdd:COG5238   331 GIGAQGAIALAKALQENTTLHSLDlSDNQ---IGDEGAIALAKYLEGNTTLRE 380
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 93-187 4.21e-07

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: 50.05  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  93 PELEEVNLNNIRnIPIPTLKAYAEALKENSY-VKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLV 171
Cdd:cd00116   108 SSLQELKLNNNG-LGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALA 186

                          90
                  ....*....|....*.
gi 1958774800 172 EALPHNTSLVELKIDN 187
Cdd:cd00116   187 EGLKANCNLEVLDLNN 202
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 6-41 1.05e-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: 66.54  E-value: 1.05e-13
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1958774800   6 ESVTLEPELEEALANASDAELCDIAAILGMHTLMSN 41
Cdd:pfam03250 107 EAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 81-212 7.09e-11

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: 61.73  E-value: 7.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  81 VEETLERIKNNDpELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 160
Cdd:COG5238   253 VIALAEALKNNT-TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958774800 161 FISGAGILCLVEALPHNTSLVELK-IDNQsqpLGNKVEMEIVNMLEKNTTLLK 212
Cdd:COG5238   331 GIGAQGAIALAKALQENTTLHSLDlSDNQ---IGDEGAIALAKYLEGNTTLRE 380
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 83-225 6.94e-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: 52.48  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  83 ETLERIKNndpeLEEVNLNNIrNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFI 162
Cdd:COG5238   286 KALQGNTT----LTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958774800 163 SGAGILCLVEALPHNTSLVELKI-DNQsqpLGNKVEMEIVNMLEKNT-TLLKFGYHFTQQGPRLR 225
Cdd:COG5238   361 GDEGAIALAKYLEGNTTLRELNLgKNN---IGKQGAEALIDALQTNRlHTLILDGNLIGAEAQQR 422
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 111-210 8.49e-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: 52.48  E-value: 8.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800 111 LKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLVEALPHNTSLVELKI-DNQs 189
Cdd:COG5238   225 AEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR- 303

                          90       100
                  ....*....|....*....|.
gi 1958774800 190 qpLGNKVEMEIVNMLEKNTTL 210
Cdd:COG5238   304 --IGDEGAIALAEGLQGNKTL 322
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 90-210 1.69e-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: 51.33  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  90 NNDPELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILC 169
Cdd:COG5238   177 LQNNSVETVYLGC-NQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1958774800 170 LVEALPHNTSLVELKIDnqsqplGNKVEME----IVNMLEKNTTL 210
Cdd:COG5238   256 LAEALKNNTTVETLYLS------GNQIGAEgaiaLAKALQGNTTL 294
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 93-187 4.21e-07

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: 50.05  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800  93 PELEEVNLNNIRnIPIPTLKAYAEALKENSY-VKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLV 171
Cdd:cd00116   108 SSLQELKLNNNG-LGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALA 186

                          90
                  ....*....|....*.
gi 1958774800 172 EALPHNTSLVELKIDN 187
Cdd:cd00116   187 EGLKANCNLEVLDLNN 202
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 111-212 3.32e-06

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: 47.35  E-value: 3.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958774800 111 LKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLVEALPHNTSLVELKIDNqsQ 190
Cdd:cd00116   154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD--N 231

                          90       100
                  ....*....|....*....|...
gi 1958774800 191 PLGNKVEMEIVN-MLEKNTTLLK 212
Cdd:cd00116   232 NLTDAGAAALASaLLSPNISLLT 254
 
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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