NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|17505500|ref|NP_491735|]
View 

Tropomodulin [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 45-191 3.45e-46

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: 155.52  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500    45 YNKGLK---DNDIEGLLSSLSIDELEDLNN---DFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWE 118
Cdd:pfam03250   1 YKKDLKkydDIDEDELLKKLSEEELEQLDElleELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17505500   119 DVCPYTpGQKRGKVYDSDSGRNSEEPENGKMEMPieidldddeeELECALVTAPEKDLVDLAGILGMHNVLNQ 191
Cdd:pfam03250  81 DVVPFT-GEKRGKVFVPKEVPDPIIEEEAITLDP----------ELEEALSSATEEELCDLAAILGMHSMMNQ 142
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 245-395 1.19e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


The actual alignment was detected with superfamily member cd00116:

Pssm-ID: 455733 [Multi-domain]  Cd Length: 319  Bit Score: 43.50  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500 245 TDLKEVNI-NNmkRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLL 323
Cdd:cd00116 165 RDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505500 324 RSTLVTQSIVefkadnQRQSVLGNQVE----MDMMMAIEENESLLRVGISFASMEARHRVSEALERNYERVRLRRL 395
Cdd:cd00116 243 SALLSPNISL------LTLSLSCNDITddgaKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 45-191 3.45e-46

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: 155.52  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500    45 YNKGLK---DNDIEGLLSSLSIDELEDLNN---DFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWE 118
Cdd:pfam03250   1 YKKDLKkydDIDEDELLKKLSEEELEQLDElleELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17505500   119 DVCPYTpGQKRGKVYDSDSGRNSEEPENGKMEMPieidldddeeELECALVTAPEKDLVDLAGILGMHNVLNQ 191
Cdd:pfam03250  81 DVVPFT-GEKRGKVFVPKEVPDPIIEEEAITLDP----------ELEEALSSATEEELCDLAAILGMHSMMNQ 142
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 245-395 1.19e-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: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500 245 TDLKEVNI-NNmkRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLL 323
Cdd:cd00116 165 RDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505500 324 RSTLVTQSIVefkadnQRQSVLGNQVE----MDMMMAIEENESLLRVGISFASMEARHRVSEALERNYERVRLRRL 395
Cdd:cd00116 243 SALLSPNISL------LTLSLSCNDITddgaKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 254-400 5.18e-03

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: 39.00  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500 254 NMKRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPElLARLLRSTLVTQSIV 333
Cdd:COG5238 272 SGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQ-GAIALAKALQENTTL 350

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17505500 334 EFK--ADNQrqsvLGNQVEMDMMMAIEENESLLRVGISFASMEARHRVS--EALERNyervRLRRLGKDPN 400
Cdd:COG5238 351 HSLdlSDNQ----IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAliDALQTN----RLHTLILDGN 413
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 45-191 3.45e-46

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: 155.52  E-value: 3.45e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500    45 YNKGLK---DNDIEGLLSSLSIDELEDLNN---DFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWE 118
Cdd:pfam03250   1 YKKDLKkydDIDEDELLKKLSEEELEQLDElleELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17505500   119 DVCPYTpGQKRGKVYDSDSGRNSEEPENGKMEMPieidldddeeELECALVTAPEKDLVDLAGILGMHNVLNQ 191
Cdd:pfam03250  81 DVVPFT-GEKRGKVFVPKEVPDPIIEEEAITLDP----------ELEEALSSATEEELCDLAAILGMHSMMNQ 142
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 245-395 1.19e-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: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500 245 TDLKEVNI-NNmkRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLL 323
Cdd:cd00116 165 RDLKELNLaNN--GIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALA 242

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17505500 324 RSTLVTQSIVefkadnQRQSVLGNQVE----MDMMMAIEENESLLRVGISFASMEARHRVSEALERNYERVRLRRL 395
Cdd:cd00116 243 SALLSPNISL------LTLSLSCNDITddgaKDLAEVLAEKESLLELDLRGNKFGEEGAQLLAESLLEPGNELESL 312
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 254-400 5.18e-03

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: 39.00  E-value: 5.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17505500 254 NMKRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPElLARLLRSTLVTQSIV 333
Cdd:COG5238 272 SGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLNLAYNGIGAQ-GAIALAKALQENTTL 350

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17505500 334 EFK--ADNQrqsvLGNQVEMDMMMAIEENESLLRVGISFASMEARHRVS--EALERNyervRLRRLGKDPN 400
Cdd:COG5238 351 HSLdlSDNQ----IGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEAliDALQTN----RLHTLILDGN 413
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH