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Conserved domains on  [gi|966935470|ref|XP_014990318|]
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leiomodin-2 isoform X2 [Macaca mulatta]

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 ...
 6-85 5.49e-14

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: 69.24  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470    6 YRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRN-LPVGLRQKSLTEKTPTGTFSREALMAYWEKesQKLLEKE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNAlLPAGQRQRDQTKKEPTGPFDREKLLHHLEK--QALEPKD 78


                  .
gi 966935470   85 R 85
Cdd:pfam03250  79 R 79
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 222-331 4.10e-13

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: 71.36  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 222 NITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHNTVLTELr 301
Cdd:COG5238  219 PIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL- 297

                         90       100       110
                 ....*....|....*....|....*....|
gi 966935470 302 FHNQRHImGSQVEMEIVKLLKENTTLLRLG 331
Cdd:COG5238  298 DLSVNRI-GDEGAIALAEGLQGNKTLHTLN 326
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 6-85 5.49e-14

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: 69.24  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470    6 YRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRN-LPVGLRQKSLTEKTPTGTFSREALMAYWEKesQKLLEKE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNAlLPAGQRQRDQTKKEPTGPFDREKLLHHLEK--QALEPKD 78


                  .
gi 966935470   85 R 85
Cdd:pfam03250  79 R 79
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 222-331 4.10e-13

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: 71.36  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 222 NITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHNTVLTELr 301
Cdd:COG5238  219 PIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL- 297

                         90       100       110
                 ....*....|....*....|....*....|
gi 966935470 302 FHNQRHImGSQVEMEIVKLLKENTTLLRLG 331
Cdd:COG5238  298 DLSVNRI-GDEGAIALAEGLQGNKTLHTLN 326
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 222-331 8.12e-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: 8.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 222 NITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHNTVLTELR 301
Cdd:cd00116  148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLN 227

                         90       100       110
                 ....*....|....*....|....*....|..
gi 966935470 302 F-HNQrhiMGSQVEMEIVK-LLKENTTLLRLG 331
Cdd:cd00116  228 LgDNN---LTDAGAAALASaLLSPNISLLTLS 256
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 6-85 5.49e-14

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: 69.24  E-value: 5.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470    6 YRRGLSKYESIDEDELLASLSAEELKELERELEDIEPDRN-LPVGLRQKSLTEKTPTGTFSREALMAYWEKesQKLLEKE 84
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDELLEELDPDNAlLPAGQRQRDQTKKEPTGPFDREKLLHHLEK--QALEPKD 78


                  .
gi 966935470   85 R 85
Cdd:pfam03250  79 R 79
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 222-331 4.10e-13

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: 71.36  E-value: 4.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 222 NITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHNTVLTELr 301
Cdd:COG5238  219 PIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSL- 297

                         90       100       110
                 ....*....|....*....|....*....|
gi 966935470 302 FHNQRHImGSQVEMEIVKLLKENTTLLRLG 331
Cdd:COG5238  298 DLSVNRI-GDEGAIALAEGLQGNKTLHTLN 326
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 215-332 6.19e-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: 64.43  E-value: 6.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 215 VNLNNIEnITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHN 294
Cdd:COG5238  185 VYLGCNQ-IGDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNN 263

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 966935470 295 TVLTELRF-HNQrhiMGSQVEMEIVKLLKENTTL--LRLGY 332
Cdd:COG5238  264 TTVETLYLsGNQ---IGAEGAIALAKALQGNTTLtsLDLSV 301
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 222-330 4.39e-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: 61.73  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 222 NITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHNTVLTELr 301
Cdd:COG5238  275 QIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSL- 353

                         90       100       110
                 ....*....|....*....|....*....|...
gi 966935470 302 fhnqrHIMGSQVEME----IVKLLKENTTLLRL 330
Cdd:COG5238  354 -----DLSDNQIGDEgaiaLAKYLEGNTTLREL 381
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 201-349 1.56e-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: 53.64  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 201 ALDKIKSNDPDTTEVNLNNIeNITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFIT 280
Cdd:COG5238  283 ALAKALQGNTTLTSLDLSVN-RIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIG 361

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 281 GKGILAIMRALQHNTVLTELrfHNQRHIMGSQVEMEIVKLLKENT-TLLRLGYHFELPGPRMSMTSILTR 349
Cdd:COG5238  362 DEGAIALAKYLEGNTTLREL--NLGKNNIGKQGAEALIDALQTNRlHTLILDGNLIGAEAQQRLEQLLER 429
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 222-331 8.12e-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: 8.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966935470 222 NITTQTLTRFAEALKDNTVVKTFSLANTHADDSAAMAIAEMLKVNEHITNINVDSNFITGKGILAIMRALQHNTVLTELR 301
Cdd:cd00116  148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLN 227

                         90       100       110
                 ....*....|....*....|....*....|..
gi 966935470 302 F-HNQrhiMGSQVEMEIVK-LLKENTTLLRLG 331
Cdd:cd00116  228 LgDNN---LTDAGAAALASaLLSPNISLLTLS 256
 
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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