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Conserved domains on  [gi|7657649|ref|NP_055362|]
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tropomodulin-3 [Homo sapiens]

Protein Classification

Tropomodulin domain-containing protein( domain architecture ID 10505465)

Tropomodulin domain-containing protein

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 ...
 5-146 1.85e-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: 218.69  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649      5 FRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSTTGPFDREHLLSYLEKEALEHKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657649     85 DYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 199-317 2.13e-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: 64.81  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  199 HLVEVNLNNIKNipiPTLKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDA 278
Cdd:COG5238 267 ETLYLSGNQIGA---EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA 343

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7657649  279 LRDNETLAELK-IDNqrqQLGTAVELEMAKMLEENTNILK 317
Cdd:COG5238 344 LQENTTLHSLDlSDN---QIGDEGAIALAKYLEGNTTLRE 380
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 5-146 1.85e-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: 218.69  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649      5 FRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSTTGPFDREHLLSYLEKEALEHKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657649     85 DYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 199-317 2.13e-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: 64.81  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  199 HLVEVNLNNIKNipiPTLKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDA 278
Cdd:COG5238 267 ETLYLSGNQIGA---EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA 343

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7657649  279 LRDNETLAELK-IDNqrqQLGTAVELEMAKMLEENTNILK 317
Cdd:COG5238 344 LQENTTLHSLDlSDN---QIGDEGAIALAKYLEGNTTLRE 380
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 216-292 4.44e-04

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: 41.57  E-value: 4.44e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7657649  216 LKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDN 292
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 5-146 1.85e-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: 218.69  E-value: 1.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649      5 FRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSTTGPFDREHLLSYLEKEALEHKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657649     85 DYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 199-317 2.13e-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: 64.81  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  199 HLVEVNLNNIKNipiPTLKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDA 278
Cdd:COG5238 267 ETLYLSGNQIGA---EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA 343

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 7657649  279 LRDNETLAELK-IDNqrqQLGTAVELEMAKMLEENTNILK 317
Cdd:COG5238 344 LQENTTLHSLDlSDN---QIGDEGAIALAKYLEGNTTLRE 380
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 191-315 3.45e-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: 3.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  191 KRTKENDAHLVEVNLNNIKNIPIptlKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGV 270
Cdd:COG5238 175 KALQNNSVETVYLGCNQIGDEGI---EELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDE 251

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7657649  271 GILALIDALRDNETLAELKIDNQRQQLGTAVELemAKMLEENTNI 315
Cdd:COG5238 252 GVIALAEALKNNTTVETLYLSGNQIGAEGAIAL--AKALQGNTTL 294
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 219-315 1.54e-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: 55.95  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  219 FAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDNqrQQLG 298
Cdd:COG5238 256 LAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY--NGIG 333

                        90
                ....*....|....*..
gi 7657649  299 TAVELEMAKMLEENTNI 315
Cdd:COG5238 334 AQGAIALAKALQENTTL 350
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 216-315 3.56e-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: 51.71  E-value: 3.56e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  216 LKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKI-DNqr 294
Cdd:COG5238 225 AEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVN-- 302

                        90       100
                ....*....|....*....|.
gi 7657649  295 qQLGTAVELEMAKMLEENTNI 315
Cdd:COG5238 303 -RIGDEGAIALAEGLQGNKTL 322
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 188-313 9.05e-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: 50.17  E-value: 9.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  188 ESLKRTKENDAHLVEVNLNNIkNIPIPTLKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFI 267
Cdd:COG5238 282 IALAKALQGNTTLTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQI 360

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 7657649  268 TGVGILALIDALRDNETLaeLKIDNQRQQLGTAVELEMAKMLEENT 313
Cdd:COG5238 361 GDEGAIALAKYLEGNTTL--RELNLGKNNIGKQGAEALIDALQTNR 404
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 188-291 1.64e-06

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: 49.40  E-value: 1.64e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  188 ESLKRTKEndahLVEVNL--NNIKNIPIPTLkdfAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESN 265
Cdd:COG5238 314 EGLQGNKT----LHTLNLayNGIGAQGAIAL---AKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKN 386

                        90       100
                ....*....|....*....|....*.
gi 7657649  266 FITGVGILALIDALRDNeTLAELKID 291
Cdd:COG5238 387 NIGKQGAEALIDALQTN-RLHTLILD 411
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 216-292 4.44e-04

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: 41.57  E-value: 4.44e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 7657649  216 LKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDN 292
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 200-280 2.75e-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: 39.26  E-value: 2.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657649  200 LVEVNL--NNIKNIPIPTLkdfAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALID 277
Cdd:cd00116 167 LKELNLanNGIGDAGIRAL---AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243


                ...
gi 7657649  278 ALR 280
Cdd:cd00116 244 ALL 246
 
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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