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Conserved domains on  [gi|388490380|ref|NP_001253348|]
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tropomodulin-3 [Macaca mulatta]

Protein Classification

tropomodulin family protein( domain architecture ID 10505465)

tropomodulin family protein such as leiomodin, an actin-binding protein that acts as an actin filament nucleator in muscle cells

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 2.30e-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: 2.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380    5 FRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSATGPFDREHLLSYLEKEALEHKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388490380   85 DYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 210-317 4.10e-12

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: 66.74  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 210 NIPIPTLKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELK 289
Cdd:COG5238  275 QIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354

                         90       100
                 ....*....|....*....|....*....
gi 388490380 290 -IDNqrqQLGTAVELEMAKMLEENTNILK 317
Cdd:COG5238  355 lSDN---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 2.30e-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: 2.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380    5 FRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSATGPFDREHLLSYLEKEALEHKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388490380   85 DYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 210-317 4.10e-12

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: 66.74  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 210 NIPIPTLKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELK 289
Cdd:COG5238  275 QIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354

                         90       100
                 ....*....|....*....|....*....
gi 388490380 290 -IDNqrqQLGTAVELEMAKMLEENTNILK 317
Cdd:COG5238  355 lSDN---QIGDEGAIALAKYLEGNTTLRE 380
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 216-292 3.19e-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: 41.96  E-value: 3.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388490380 216 LKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDN 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 2.30e-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: 2.30e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380    5 FRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSATGPFDREHLLSYLEKEALEHKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 388490380   85 DYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 210-317 4.10e-12

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: 66.74  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 210 NIPIPTLKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELK 289
Cdd:COG5238  275 QIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLD 354

                         90       100
                 ....*....|....*....|....*....
gi 388490380 290 -IDNqrqQLGTAVELEMAKMLEENTNILK 317
Cdd:COG5238  355 lSDN---QIGDEGAIALAKYLEGNTTLRE 380
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 216-315 6.76e-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: 57.11  E-value: 6.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 216 LKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDNQRQ 295
Cdd:COG5238  197 IEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQI 276

                         90       100
                 ....*....|....*....|
gi 388490380 296 QLGTAVELemAKMLEENTNI 315
Cdd:COG5238  277 GAEGAIAL--AKALQGNTTL 294
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 219-315 1.05e-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: 56.34  E-value: 1.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 219 FAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDNqrQQLG 298
Cdd:COG5238  256 LAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAY--NGIG 333

                         90
                 ....*....|....*..
gi 388490380 299 TAVELEMAKMLEENTNI 315
Cdd:COG5238  334 AQGAIALAKALQENTTL 350
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 216-315 2.58e-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: 52.10  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 216 LKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKI-DNqr 294
Cdd:COG5238  225 AEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVN-- 302

                         90       100
                 ....*....|....*....|.
gi 388490380 295 qQLGTAVELEMAKMLEENTNI 315
Cdd:COG5238  303 -RIGDEGAIALAEGLQGNKTL 322
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 195-291 1.53e-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: 49.79  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 195 ENDAYLVEVNL--NNIKNIPIPTLkdfAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGI 272
Cdd:COG5238  317 QGNKTLHTLNLayNGIGAQGAIAL---AKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGA 393

                         90
                 ....*....|....*....
gi 388490380 273 LALIDALRDNeTLAELKID 291
Cdd:COG5238  394 EALIDALQTN-RLHTLILD 411
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 204-330 2.38e-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: 49.02  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 204 NLNNIKNipiPTLKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNE 283
Cdd:COG5238  300 SVNRIGD---EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNT 376

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 388490380 284 TLaeLKIDNQRQQLGTAVELEMAKMLEENTNI-LKFGYQFTQQGPRTR 330
Cdd:COG5238  377 TL--RELNLGKNNIGKQGAEALIDALQTNRLHtLILDGNLIGAEAQQR 422
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 216-292 3.19e-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: 41.96  E-value: 3.19e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 388490380 216 LKDFAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDN 292
Cdd:cd00116  154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 200-280 1.52e-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: 40.03  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 388490380 200 LVEVNL--NNIKNIPIPTLkdfAKALETNTHVKYFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALID 277
Cdd:cd00116  167 LKELNLanNGIGDAGIRAL---AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243


                 ...
gi 388490380 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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