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Conserved domains on  [gi|397174804|ref|NP_001257579|]
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tropomodulin-4 [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 ...
 4-143 5.33e-67

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: 207.14  E-value: 5.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804    4 YQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERD 83
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 397174804   84 DLVPFTGEKKGKPFI--QPKREIPAQEQITLEPELEEALSHATDAEMCDIAAILGMYTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVpkEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 194-285 1.06e-08

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: 56.34  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 194 DKELEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISSTGLMA 271
Cdd:COG5238  179 NNSVETVYLgcNQIGDEGIEEL---AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                         90
                 ....*....|....
gi 397174804 272 VLKAVRENATLTEL 285
Cdd:COG5238  256 LAEALKNNTTVETL 269
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 4-143 5.33e-67

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: 207.14  E-value: 5.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804    4 YQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERD 83
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 397174804   84 DLVPFTGEKKGKPFI--QPKREIPAQEQITLEPELEEALSHATDAEMCDIAAILGMYTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVpkEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 194-285 1.06e-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: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 194 DKELEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISSTGLMA 271
Cdd:COG5238  179 NNSVETVYLgcNQIGDEGIEEL---AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                         90
                 ....*....|....
gi 397174804 272 VLKAVRENATLTEL 285
Cdd:COG5238  256 LAEALKNNTTVETL 269
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 184-286 1.48e-05

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: 46.19  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 184 EEMLKRVRSNDKeLEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIES 261
Cdd:cd00116  155 EALAKALRANRD-LKELNLanNGIGDAGIRAL---AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230

                         90       100
                 ....*....|....*....|....*.
gi 397174804 262 NFISSTGLMAVLKAVR-ENATLTELR 286
Cdd:cd00116  231 NNLTDAGAAALASALLsPNISLLTLS 256
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 4-143 5.33e-67

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: 207.14  E-value: 5.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804    4 YQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERD 83
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 397174804   84 DLVPFTGEKKGKPFI--QPKREIPAQEQITLEPELEEALSHATDAEMCDIAAILGMYTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVpkEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 194-285 1.06e-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: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 194 DKELEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISSTGLMA 271
Cdd:COG5238  179 NNSVETVYLgcNQIGDEGIEEL---AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                         90
                 ....*....|....
gi 397174804 272 VLKAVRENATLTEL 285
Cdd:COG5238  256 LAEALKNNTTVETL 269
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 216-285 2.44e-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: 55.18  E-value: 2.44e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 216 LCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISSTGLMAVLKAVRENATLTEL 285
Cdd:COG5238  228 LAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL 297
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 193-312 6.13e-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: 50.94  E-value: 6.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 193 NDKELEEVNL--NNIQDipiPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISSTGLM 270
Cdd:COG5238  262 NNTTVETLYLsgNQIGA---EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAI 338

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 397174804 271 AVLKAVRENATLTELRV-DNQRqwpGDAVEMEMATVLEQCPSI 312
Cdd:COG5238  339 ALAKALQENTTLHSLDLsDNQI---GDEGAIALAKYLEGNTTL 378
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 183-285 8.90e-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: 47.09  E-value: 8.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 183 IEEMLKRvrsnDKELEEVNLNNIQdIPIPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESN 262
Cdd:COG5238  228 LAEALKG----NKSLTTLDLSNNQ-IGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVN 302

                         90       100
                 ....*....|....*....|...
gi 397174804 263 FISSTGLMAVLKAVRENATLTEL 285
Cdd:COG5238  303 RIGDEGAIALAEGLQGNKTLHTL 325
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 192-285 1.21e-05

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: 46.71  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 192 SNDKELEEVNL--NNIQDipiPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISSTGL 269
Cdd:COG5238  289 QGNTTLTSLDLsvNRIGD---EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGA 365

                         90
                 ....*....|....*.
gi 397174804 270 MAVLKAVRENATLTEL 285
Cdd:COG5238  366 IALAKYLEGNTTLREL 381
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 184-286 1.48e-05

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: 46.19  E-value: 1.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 184 EEMLKRVRSNDKeLEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIES 261
Cdd:cd00116  155 EALAKALRANRD-LKELNLanNGIGDAGIRAL---AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230

                         90       100
                 ....*....|....*....|....*.
gi 397174804 262 NFISSTGLMAVLKAVR-ENATLTELR 286
Cdd:cd00116  231 NNLTDAGAAALASALLsPNISLLTLS 256
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 193-312 1.82e-05

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: 46.32  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 397174804 193 NDKELEEVNL--NNIQD---IPipvlsdLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLLSLNIESNFISST 267
Cdd:COG5238  318 GNKTLHTLNLayNGIGAqgaIA------LAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQ 391

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 397174804 268 GLMAVLKAVRENaTLTELRVDnqrqwPGDAVEMEMATVLEQCPSI 312
Cdd:COG5238  392 GAEALIDALQTN-RLHTLILD-----GNLIGAEAQQRLEQLLERI 430
 
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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