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Conserved domains on  [gi|52219160|ref|NP_001004608|]
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tropomodulin-2 [Danio rerio]

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 3.21e-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: 207.91  E-value: 3.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160     5 FKKDLEKYKEIDEDEILNKLSEEELKQLESALEEIDPENALLPAGLRQKDQTSKTDTGPFNRDKLLQYLEKEALDYKERE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52219160    85 DIVPFTGEKKGKVWIPKQKPIQLHQEEATTLDPELEEALSSATDTELHDLAAILGVNTLVTS 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 192-308 7.91e-14

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: 72.13  E-value: 7.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 192 TLTGVNLNNiKNIPIPTLKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEA 271
Cdd:COG5238 265 TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA 343

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 52219160 272 LRDNDTLSEIK-IDNqrqQLGTSAEMEIAKMLEQNTSI 308
Cdd:COG5238 344 LQENTTLHSLDlSDN---QIGDEGAIALAKYLEGNTTL 378
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 5-146 3.21e-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: 207.91  E-value: 3.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160     5 FKKDLEKYKEIDEDEILNKLSEEELKQLESALEEIDPENALLPAGLRQKDQTSKTDTGPFNRDKLLQYLEKEALDYKERE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52219160    85 DIVPFTGEKKGKVWIPKQKPIQLHQEEATTLDPELEEALSSATDTELHDLAAILGVNTLVTS 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 192-308 7.91e-14

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: 72.13  E-value: 7.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 192 TLTGVNLNNiKNIPIPTLKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEA 271
Cdd:COG5238 265 TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA 343

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 52219160 272 LRDNDTLSEIK-IDNqrqQLGTSAEMEIAKMLEQNTSI 308
Cdd:COG5238 344 LQENTTLHSLDlSDN---QIGDEGAIALAKYLEGNTTL 378
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 209-285 5.92e-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: 44.27  E-value: 5.92e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52219160 209 LKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEALRDNDTLSEIKIDN 285
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
247-274 2.79e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 2.79e-04
                           10        20
                   ....*....|....*....|....*...
gi 52219160    247 NKTLRSLNLESNFITGAGVQALVEALRD 274
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 5-146 3.21e-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: 207.91  E-value: 3.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160     5 FKKDLEKYKEIDEDEILNKLSEEELKQLESALEEIDPENALLPAGLRQKDQTSKTDTGPFNRDKLLQYLEKEALDYKERE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52219160    85 DIVPFTGEKKGKVWIPKQKPIQLHQEEATTLDPELEEALSSATDTELHDLAAILGVNTLVTS 146
Cdd:pfam03250  81 DVVPFTGEKRGKVFVPKEVPDPIIEEEAITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 192-308 7.91e-14

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: 72.13  E-value: 7.91e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 192 TLTGVNLNNiKNIPIPTLKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEA 271
Cdd:COG5238 265 TVETLYLSG-NQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKA 343

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 52219160 272 LRDNDTLSEIK-IDNqrqQLGTSAEMEIAKMLEQNTSI 308
Cdd:COG5238 344 LQENTTLHSLDlSDN---QIGDEGAIALAKYLEGNTTL 378
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 190-308 1.09e-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: 62.50  E-value: 1.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 190 DPTLTGVNLNNiKNIPIPTLKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALV 269
Cdd:COG5238 179 NNSVETVYLGC-NQIGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALA 257

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 52219160 270 EALRDNDTLSeiKIDNQRQQLGTSAEMEIAKMLEQNTSI 308
Cdd:COG5238 258 EALKNNTTVE--TLYLSGNQIGAEGAIALAKALQGNTTL 294
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 102-326 1.28e-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: 62.11  E-value: 1.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 102 QKPIQLHQEEATTLDPELEEALSSATDTELHDLAAI-LGVNTLVTSTQSYDGSKDGYNNVIKGEKVKPVfdEPPNPTNVE 180
Cdd:COG5238 114 TPPPDLRRIMAKTLEDSLILYLALPRRINLIQVLKDpLGGNAVHLLGLAARLGLLAAISMAKALQNNSV--ETVYLGCNQ 191

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 181 ESLQRIKA------NDPTLTGVNLNNiKNIPIPTLKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLN 254
Cdd:COG5238 192 IGDEGIEElaealtQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLY 270

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52219160 255 LESNFITGAGVQALVEALRDNDTLSEIKI-DNqrqQLGTSAEMEIAKMLEQNTSIVKFGYHFTQ---QGPRSRAAA 326
Cdd:COG5238 271 LSGNQIGAEGAIALAKALQGNTTLTSLDLsVN---RIGDEGAIALAEGLQGNKTLHTLNLAYNGigaQGAIALAKA 343
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 188-328 5.24e-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: 60.19  E-value: 5.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 188 ANDPTLTGVNLNNIkNIPIPTLKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQA 267
Cdd:COG5238 289 QGNTTLTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIA 367

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 52219160 268 LVEALRDNDTLseIKIDNQRQQLGTSAEMEIAKMLEQNTSI-VKFGYHFTQQGPRSRAAAAI 328
Cdd:COG5238 368 LAKYLEGNTTL--RELNLGKNNIGKQGAEALIDALQTNRLHtLILDGNLIGAEAQQRLEQLL 427
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 209-285 5.92e-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: 44.27  E-value: 5.92e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52219160 209 LKELAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEALRDNDTLSEIKIDN 285
Cdd:cd00116 154 CEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGD 230
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 212-312 1.26e-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: 43.11  E-value: 1.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52219160 212 LAKAMERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEALR-DNDTLSEIKIDNqrQQL 290
Cdd:cd00116 185 LAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLsPNISLLTLSLSC--NDI 262

                        90       100
                ....*....|....*....|..
gi 52219160 291 GTSAEMEIAKMLEQNTSIVKFG 312
Cdd:cd00116 263 TDDGAKDLAEVLAEKESLLELD 284
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 209-285 2.57e-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: 42.34  E-value: 2.57e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52219160 209 LKELAKAM-ERNTHVKKFSLAATRSNDPVAVAFSDMLRENKTLRSLNLESNFITGAGVQALVEALRDNDTLSEIKIDN 285
Cdd:cd00116 125 LRLLAKGLkDLPPALEKLVLGRNRLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNN 202
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
247-274 2.79e-04

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 2.79e-04
                           10        20
                   ....*....|....*....|....*...
gi 52219160    247 NKTLRSLNLESNFITGAGVQALVEALRD 274
Cdd:smart00368   1 NPSLRELDLSNNKLGDEGARALAEALKD 28
 
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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