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Conserved domains on  [gi|2024353443|ref|XP_015148734|]
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leiomodin-3 [Gallus gallus]

Protein Classification

leucine-rich repeat domain-containing protein( domain architecture ID 1903313)

leucine-rich repeat (LRR) domain-containing protein may participate in protein-protein interactions

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Tropomodulin super family cl12276
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 15-92 5.60e-13

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.


The actual alignment was detected with superfamily member pfam03250:

Pssm-ID: 460862  Cd Length: 142  Bit Score: 66.16  E-value: 5.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024353443  15 EDINEDEILANLSPEELKELQSEMEVMAPD-PELPTGMIQRDQTEKPPTGSFDHRSLVDYLYwQKASRRMLEDERVPVT 92
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHHLE-KQALEPKDREDVVPFT 86
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 232-371 7.89e-11

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: 64.04  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 232 SGNQTNLE--ESLEKVRKNNPDMKELNLNNiENIPKEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENRSI 309
Cdd:COG5238   188 GCNQIGDEgiEELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024353443 310 TTLNIDSNFISGKGVVAIMRCLQYNEMLTEFRF-HNQrsmLGHQAEMEIARLLKANNTLLKMG 371
Cdd:COG5238   267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 15-92 5.60e-13

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: 66.16  E-value: 5.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024353443  15 EDINEDEILANLSPEELKELQSEMEVMAPD-PELPTGMIQRDQTEKPPTGSFDHRSLVDYLYwQKASRRMLEDERVPVT 92
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHHLE-KQALEPKDREDVVPFT 86
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 232-371 7.89e-11

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: 64.04  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 232 SGNQTNLE--ESLEKVRKNNPDMKELNLNNiENIPKEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENRSI 309
Cdd:COG5238   188 GCNQIGDEgiEELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024353443 310 TTLNIDSNFISGKGVVAIMRCLQYNEMLTEFRF-HNQrsmLGHQAEMEIARLLKANNTLLKMG 371
Cdd:COG5238   267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 240-327 2.24e-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: 43.50  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 240 ESLEKVRKNNPDMKELNL-NNieNIPKEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENRSITTLNIDSNF 318
Cdd:cd00116   155 EALAKALRANRDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN 232


                  ....*....
gi 2024353443 319 ISGKGVVAI 327
Cdd:cd00116   233 LTDAGAAAL 241
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 15-92 5.60e-13

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: 66.16  E-value: 5.60e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024353443  15 EDINEDEILANLSPEELKELQSEMEVMAPD-PELPTGMIQRDQTEKPPTGSFDHRSLVDYLYwQKASRRMLEDERVPVT 92
Cdd:pfam03250   9 DDIDEDELLKKLSEEELEQLDELLEELDPDnALLPAGQRQRDQTKKEPTGPFDREKLLHHLE-KQALEPKDREDVVPFT 86
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 232-371 7.89e-11

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: 64.04  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 232 SGNQTNLE--ESLEKVRKNNPDMKELNLNNiENIPKEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENRSI 309
Cdd:COG5238   188 GCNQIGDEgiEELAEALTQNTTVTTLWLKR-NPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTV 266

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024353443 310 TTLNIDSNFISGKGVVAIMRCLQYNEMLTEFRF-HNQrsmLGHQAEMEIARLLKANNTLLKMG 371
Cdd:COG5238   267 ETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLsVNR---IGDEGAIALAEGLQGNKTLHTLN 326
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 255-367 4.29e-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: 58.65  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 255 LNLNNIENipkEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENRSITTLNIDSNFISGKGVVAIMRCLQYN 334
Cdd:COG5238   187 LGCNQIGD---EGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2024353443 335 EMLTEFRF-HNQrsmLGHQAEMEIARLLKANNTL 367
Cdd:COG5238   264 TTVETLYLsGNQ---IGAEGAIALAKALQGNTTL 294
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 232-370 4.91e-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: 4.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 232 SGNQTNLE--ESLEKVRKNNPDMKELNL--NNIENipkEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENR 307
Cdd:COG5238   244 SNNQIGDEgvIALAEALKNNTTVETLYLsgNQIGA---EGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNK 320

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024353443 308 SITTLNIDSNFISGKGVVAIMRCLQYNEMLTefRFHNQRSMLGHQAEMEIARLLKANNTLLKM 370
Cdd:COG5238   321 TLHTLNLAYNGIGAQGAIALAKALQENTTLH--SLDLSDNQIGDEGAIALAKYLEGNTTLREL 381
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 227-334 1.23e-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: 44.78  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 227 LSARPSGNQ--TNLEESLEKvrknNPDMKELNL--NNIENIPKEMLIDfvnAMKKNKNIKTFSLANVGADDNVAFALANM 302
Cdd:COG5238   299 LSVNRIGDEgaIALAEGLQG----NKTLHTLNLayNGIGAQGAIALAK---ALQENTTLHSLDLSDNQIGDEGAIALAKY 371

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2024353443 303 LRENRSITTLNIDSNFISGKGVVAIMRCLQYN 334
Cdd:COG5238   372 LEGNTTLRELNLGKNNIGKQGAEALIDALQTN 403
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 240-327 2.24e-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: 43.50  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024353443 240 ESLEKVRKNNPDMKELNL-NNieNIPKEMLIDFVNAMKKNKNIKTFSLANVGADDNVAFALANMLRENRSITTLNIDSNF 318
Cdd:cd00116   155 EALAKALRANRDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN 232


                  ....*....
gi 2024353443 319 ISGKGVVAI 327
Cdd:cd00116   233 LTDAGAAAL 241
 
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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