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Conserved domains on  [gi|48675841|ref|NP_037176|]
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tropomodulin-1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 3-143 5.67e-71

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: 217.92  E-value: 5.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841     3 YRRELEKYRDLDEDEILGALTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFKREELLDHLEKQAKEFKDRE 82
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48675841    83 DLVPYTGEKRGKIWVPKQKPMDPVLES-VTLEPELEEALANASDAELCDIAAILGMHTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEaITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 183-314 9.55e-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: 62.89  E-value: 9.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 183 VEETLERIKNNDpELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 262
Cdd:COG5238 253 VIALAEALKNNT-TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 48675841 263 FISGAGILCLVEALPHNTSLVELK-IDNQsqpLGNKVEMEIVNMLEKNTTLLK 314
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 ...
 3-143 5.67e-71

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: 217.92  E-value: 5.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841     3 YRRELEKYRDLDEDEILGALTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFKREELLDHLEKQAKEFKDRE 82
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48675841    83 DLVPYTGEKRGKIWVPKQKPMDPVLES-VTLEPELEEALANASDAELCDIAAILGMHTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEaITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 183-314 9.55e-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: 62.89  E-value: 9.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 183 VEETLERIKNNDpELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 262
Cdd:COG5238 253 VIALAEALKNNT-TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 48675841 263 FISGAGILCLVEALPHNTSLVELK-IDNQsqpLGNKVEMEIVNMLEKNTTLLK 314
Cdd:COG5238 331 GIGAQGAIALAKALQENTTLHSLDlSDNQ---IGDEGAIALAKYLEGNTTLRE 380
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 195-289 1.35e-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: 49.28  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 195 PELEEVNLNNIRnIPIPTLKAYAEALKENSY-VKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLV 273
Cdd:cd00116 108 SSLQELKLNNNG-LGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALA 186

                        90
                ....*....|....*.
gi 48675841 274 EALPHNTSLVELKIDN 289
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 ...
 3-143 5.67e-71

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: 217.92  E-value: 5.67e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841     3 YRRELEKYRDLDEDEILGALTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFKREELLDHLEKQAKEFKDRE 82
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 48675841    83 DLVPYTGEKRGKIWVPKQKPMDPVLES-VTLEPELEEALANASDAELCDIAAILGMHTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEaITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 183-314 9.55e-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: 62.89  E-value: 9.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 183 VEETLERIKNNDpELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 262
Cdd:COG5238 253 VIALAEALKNNT-TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYN 330

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 48675841 263 FISGAGILCLVEALPHNTSLVELK-IDNQsqpLGNKVEMEIVNMLEKNTTLLK 314
Cdd:COG5238 331 GIGAQGAIALAKALQENTTLHSLDlSDNQ---IGDEGAIALAKYLEGNTTLRE 380
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 185-327 8.17e-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: 53.64  E-value: 8.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 185 ETLERIKNndpeLEEVNL--NNIRNipiPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESN 262
Cdd:COG5238 286 KALQGNTT----LTSLDLsvNRIGD---EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDN 358

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 48675841 263 FISGAGILCLVEALPHNTSLVELKI-DNQsqpLGNKVEMEIVNMLEKNT-TLLKFGYHFTQQGPRLR 327
Cdd:COG5238 359 QIGDEGAIALAKYLEGNTTLRELNLgKNN---IGKQGAEALIDALQTNRlHTLILDGNLIGAEAQQR 422
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 213-312 1.10e-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: 53.26  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 213 LKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLVEALPHNTSLVELKI-DNQs 291
Cdd:COG5238 225 AEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR- 303

                        90       100
                ....*....|....*....|.
gi 48675841 292 qpLGNKVEMEIVNMLEKNTTL 312
Cdd:COG5238 304 --IGDEGAIALAEGLQGNKTL 322
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 192-312 1.92e-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: 52.48  E-value: 1.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 192 NNDPELEEVNLNNiRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILC 271
Cdd:COG5238 177 LQNNSVETVYLGC-NQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 48675841 272 LVEALPHNTSLVELKIDnqsqplGNKVEME----IVNMLEKNTTL 312
Cdd:COG5238 256 LAEALKNNTTVETLYLS------GNQIGAEgaiaLAKALQGNTTL 294
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 195-289 1.35e-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: 49.28  E-value: 1.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 195 PELEEVNLNNIRnIPIPTLKAYAEALKENSY-VKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLV 273
Cdd:cd00116 108 SSLQELKLNNNG-LGDRGLRLLAKGLKDLPPaLEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALA 186

                        90
                ....*....|....*.
gi 48675841 274 EALPHNTSLVELKIDN 289
Cdd:cd00116 187 EGLKANCNLEVLDLNN 202
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 213-314 9.73e-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: 46.96  E-value: 9.73e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 48675841 213 LKAYAEALKENSYVKKFSIVGTRSNDPVAFALAEMLKVNKVLKTLNVESNFISGAGILCLVEALPHNTSLVELKIDNqsQ 292
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD--N 231

                        90       100
                ....*....|....*....|...
gi 48675841 293 PLGNKVEMEIVN-MLEKNTTLLK 314
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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