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Conserved domains on  [gi|218931148|ref|NP_001136357|]
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tropomodulin-2 isoform b [Homo sapiens]

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 ...
 5-146 2.88e-66

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: 204.44  E-value: 2.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148    5 FQKELEKYKNIDEDELLGKLSEEELKQLENVLDDLDPESAMLPAGFRQKDQTQKAATGPFDREHLLMYLEKEALEQKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218931148   85 DFVPFTGEKKGRVFIPKEKPIETRKEEKVTLDPELEEALASASDTELYDLAAVLGVHNLLNN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 187-302 7.28e-10

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: 59.42  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 187 ISLQQMKANDPSLQEVNL--NNI-----KAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIK-IDNqrq 258
Cdd:COG5238  282 IALAKALQGNTTLTSLDLsvNRIgdegaIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDlSDN--- 358

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 218931148 259 QLGTAVEMEIAQMLEENSRILKF---GYQFTKQGpRTRVAAAITKNN 302
Cdd:COG5238  359 QIGDEGAIALAKYLEGNTTLRELnlgKNNIGKQG-AEALIDALQTNR 404
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 5-146 2.88e-66

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: 204.44  E-value: 2.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148    5 FQKELEKYKNIDEDELLGKLSEEELKQLENVLDDLDPESAMLPAGFRQKDQTQKAATGPFDREHLLMYLEKEALEQKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218931148   85 DFVPFTGEKKGRVFIPKEKPIETRKEEKVTLDPELEEALASASDTELYDLAAVLGVHNLLNN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 187-302 7.28e-10

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: 59.42  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 187 ISLQQMKANDPSLQEVNL--NNI-----KAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIK-IDNqrq 258
Cdd:COG5238  282 IALAKALQGNTTLTSLDLsvNRIgdegaIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDlSDN--- 358

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 218931148 259 QLGTAVEMEIAQMLEENSRILKF---GYQFTKQGpRTRVAAAITKNN 302
Cdd:COG5238  359 QIGDEGAIALAKYLEGNTTLRELnlgKNNIGKQG-AEALIDALQTNR 404
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 197-287 1.05e-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: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 197 PSLQEVNLNN-------IKAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIKI-DNQRQQLGTAvemEI 268
Cdd:cd00116  165 RDLKELNLANngigdagIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLgDNNLTDAGAA---AL 241

                         90       100
                 ....*....|....*....|
gi 218931148 269 A-QMLEENSRILKFGYQFTK 287
Cdd:cd00116  242 AsALLSPNISLLTLSLSCND 261
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 5-146 2.88e-66

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: 204.44  E-value: 2.88e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148    5 FQKELEKYKNIDEDELLGKLSEEELKQLENVLDDLDPESAMLPAGFRQKDQTQKAATGPFDREHLLMYLEKEALEQKDRE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 218931148   85 DFVPFTGEKKGRVFIPKEKPIETRKEEKVTLDPELEEALASASDTELYDLAAVLGVHNLLNN 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 187-302 7.28e-10

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: 59.42  E-value: 7.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 187 ISLQQMKANDPSLQEVNL--NNI-----KAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIK-IDNqrq 258
Cdd:COG5238  282 IALAKALQGNTTLTSLDLsvNRIgdegaIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDlSDN--- 358

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 218931148 259 QLGTAVEMEIAQMLEENSRILKF---GYQFTKQGpRTRVAAAITKNN 302
Cdd:COG5238  359 QIGDEGAIALAKYLEGNTTLRELnlgKNNIGKQG-AEALIDALQTNR 404
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 188-306 2.73e-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: 48.63  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 188 SLQQMKANDPSLQEVNL--NNIK-----AFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIKI-DNqrqQ 259
Cdd:COG5238  227 ILAEALKGNKSLTTLDLsnNQIGdegviALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVN---R 303

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 218931148 260 LGTAVEMEIAQMLEENSRI--LKFGY-QFTKQGPRtRVAAAITKNNDLVR 306
Cdd:COG5238  304 IGDEGAIALAEGLQGNKTLhtLNLAYnGIGAQGAI-ALAKALQENTTLHS 352
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 208-278 9.67e-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: 43.63  E-value: 9.67e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 218931148 208 KAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTeiKIDNQRQQLGTAVEMEIAQMLEENSRI 278
Cdd:COG5238  226 EILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTL 294
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 196-278 1.33e-04

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: 43.24  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 196 DPSLQEVNLNN-------IKAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIKIDNqrQQLGTAVEMEI 268
Cdd:COG5238  179 NNSVETVYLGCnqigdegIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSN--NQIGDEGVIAL 256

                         90
                 ....*....|
gi 218931148 269 AQMLEENSRI 278
Cdd:COG5238  257 AEALKNNTTV 266
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 197-287 1.05e-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: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 197 PSLQEVNLNN-------IKAFADMLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEIKI-DNQRQQLGTAvemEI 268
Cdd:cd00116  165 RDLKELNLANngigdagIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLgDNNLTDAGAA---AL 241

                         90       100
                 ....*....|....*....|
gi 218931148 269 A-QMLEENSRILKFGYQFTK 287
Cdd:cd00116  242 AsALLSPNISLLTLSLSCND 261
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 197-281 3.11e-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: 38.88  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 218931148 197 PSLQEVNLNN-------IKAFAD-MLKVNKTLTSLNIESNFITGTGILALVEALKENDTLTEikIDNQRQQLGTAVEMEI 268
Cdd:cd00116  221 KSLEVLNLGDnnltdagAAALASaLLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKESLLE--LDLRGNKFGEEGAQLL 298

                         90
                 ....*....|...
gi 218931148 269 AQMLEENSRILKF 281
Cdd:cd00116  299 AESLLEPGNELES 311
 
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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