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Conserved domains on  [gi|7710104|ref|NP_057921|]
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tropomodulin-4 [Mus musculus]

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 4.73e-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: 207.52  E-value: 4.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104      4 YQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERD 83
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710104     84 DLVPYTGEKKGKPFI--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 5.09e-09

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: 57.11  E-value: 5.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  194 DKELEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGLMA 271
Cdd:COG5238 179 NNSVETVYLgcNQIGDEGIEEL---AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                        90
                ....*....|....
gi 7710104  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 4.73e-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: 207.52  E-value: 4.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104      4 YQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERD 83
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710104     84 DLVPYTGEKKGKPFI--QPKREIPAQEQITLEPELEEALSHATDAEMCDIAAILGMYTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVpkEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 194-285 5.09e-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: 5.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  194 DKELEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGLMA 271
Cdd:COG5238 179 NNSVETVYLgcNQIGDEGIEEL---AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                        90
                ....*....|....
gi 7710104  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 4.29e-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: 47.74  E-value: 4.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  184 EEMLKRVRSNDKeLEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIES 261
Cdd:cd00116 155 EALAKALRANRD-LKELNLanNGIGDAGIRAL---AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230

                        90       100
                ....*....|....*....|....*.
gi 7710104  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 4.73e-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: 207.52  E-value: 4.73e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104      4 YQKELEKYRDIDEDEILRTLSPEELEQLDCELQEMDPENMLLPAGLRQRDQTKKSPTGPLDRDALLQYLEQQALEVKERD 83
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7710104     84 DLVPYTGEKKGKPFI--QPKREIPAQEQITLEPELEEALSHATDAEMCDIAAILGMYTLMSN 143
Cdd:pfam03250  81 DVVPFTGEKRGKVFVpkEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 194-285 5.09e-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: 5.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  194 DKELEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGLMA 271
Cdd:COG5238 179 NNSVETVYLgcNQIGDEGIEEL---AEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIA 255

                        90
                ....*....|....
gi 7710104  272 VLKAVRENATLTEL 285
Cdd:COG5238 256 LAEALKNNTTVETL 269
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 216-285 9.37e-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: 56.34  E-value: 9.37e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  216 LCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGLMAVLKAVRENATLTEL 285
Cdd:COG5238 228 LAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL 297
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 193-312 3.86e-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: 3.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  193 NDKELEEVNL--NNIQDipiPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGLM 270
Cdd:COG5238 262 NNTTVETLYLsgNQIGA---EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAI 338

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 7710104  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 1.81e-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: 1.81e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  183 IEEMLKRvrsnDKELEEVNLNNIQdIPIPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESN 262
Cdd:COG5238 228 LAEALKG----NKSLTTLDLSNNQ-IGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVN 302

                        90       100
                ....*....|....*....|...
gi 7710104  263 FISSTGLMAVLKAVRENATLTEL 285
Cdd:COG5238 303 RIGDEGAIALAEGLQGNKTLHTL 325
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 184-286 4.29e-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: 47.74  E-value: 4.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  184 EEMLKRVRSNDKeLEEVNL--NNIQDIPIPVLsdlCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIES 261
Cdd:cd00116 155 EALAKALRANRD-LKELNLanNGIGDAGIRAL---AEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230

                        90       100
                ....*....|....*....|....*.
gi 7710104  262 NFISSTGLMAVLKAVR-ENATLTELR 286
Cdd:cd00116 231 NNLTDAGAAALASALLsPNISLLTLS 256
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 192-285 5.71e-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: 47.86  E-value: 5.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  192 SNDKELEEVNL--NNIQDipiPVLSDLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISSTGL 269
Cdd:COG5238 289 QGNTTLTSLDLsvNRIGD---EGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGA 365

                        90
                ....*....|....*.
gi 7710104  270 MAVLKAVRENATLTEL 285
Cdd:COG5238 366 IALAKYLEGNTTLREL 381
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 193-312 3.94e-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: 45.17  E-value: 3.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7710104  193 NDKELEEVNL--NNIQD---IPipvlsdLCEAMKTNTYVRSFSLVATKSGDPIANAVADMLRENRSLQSLNIESNFISST 267
Cdd:COG5238 318 GNKTLHTLNLayNGIGAqgaIA------LAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQ 391

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 7710104  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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