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Conserved domains on  [gi|17136982|ref|NP_477032|]
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tropomodulin, isoform B [Drosophila melanogaster]

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 ...
 55-197 2.25e-56

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: 181.72  E-value: 2.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982    55 YGKDLSEYDDVDVESLLAQLSPEEITILAK---EVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQP 131
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDElleELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136982   132 EFEPFvQGKVRGKKWVPPPRDARDIEAEeqiAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQ 197
Cdd:pfam03250  81 DVVPF-TGEKRGKVFVPKEVPDPIIEEE---AITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
PPP1R42 super family cl42388
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 249-332 7.31e-07

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: 50.43  E-value: 7.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 249 SKLIDLNLNNiKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQ 328
Cdd:cd00116 165 RDLKELNLAN-NGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243


                ....
gi 17136982 329 ALLK 332
Cdd:cd00116 244 ALLS 247
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 55-197 2.25e-56

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: 181.72  E-value: 2.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982    55 YGKDLSEYDDVDVESLLAQLSPEEITILAK---EVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQP 131
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDElleELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136982   132 EFEPFvQGKVRGKKWVPPPRDARDIEAEeqiAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQ 197
Cdd:pfam03250  81 DVVPF-TGEKRGKVFVPKEVPDPIIEEE---AITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 249-332 7.31e-07

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: 50.43  E-value: 7.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 249 SKLIDLNLNNiKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQ 328
Cdd:cd00116 165 RDLKELNLAN-NGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243


                ....
gi 17136982 329 ALLK 332
Cdd:cd00116 244 ALLS 247
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 252-389 8.86e-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: 47.48  E-value: 8.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 252 IDLNLNNIkniSDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALL 331
Cdd:COG5238 297 LDLSVNRI---GDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE 373

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136982 332 KCHTIEEFrasNQRSAVLGNKIEMEITDLVEKNS-SLLRLGLHLEFNDARHRVAAHLQR 389
Cdd:COG5238 374 GNTTLREL---NLGKNNIGKQGAEALIDALQTNRlHTLILDGNLIGAEAQQRLEQLLER 429
 
Name Accession Description Interval E-value
Tropomodulin pfam03250
Tropomodulin; Tropomodulin is a novel tropomyosin regulatory protein that binds to the end of ...
 55-197 2.25e-56

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: 181.72  E-value: 2.25e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982    55 YGKDLSEYDDVDVESLLAQLSPEEITILAK---EVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQP 131
Cdd:pfam03250   1 YKKDLKKYDDIDEDELLKKLSEEELEQLDElleELDPDNALLPAGQRQRDQTKKEPTGPFDREKLLHHLEKQALEPKDRE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17136982   132 EFEPFvQGKVRGKKWVPPPRDARDIEAEeqiAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQ 197
Cdd:pfam03250  81 DVVPF-TGEKRGKVFVPKEVPDPIIEEE---AITLDPELEEALSSATEEELCDLAAILGMHSMMNQ 142
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 249-332 7.31e-07

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: 50.43  E-value: 7.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 249 SKLIDLNLNNiKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQ 328
Cdd:cd00116 165 RDLKELNLAN-NGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNNLTDAGAAALAS 243


                ....
gi 17136982 329 ALLK 332
Cdd:cd00116 244 ALLS 247
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 252-389 8.86e-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: 47.48  E-value: 8.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 252 IDLNLNNIkniSDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALL 331
Cdd:COG5238 297 LDLSVNRI---GDEGAIALAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLE 373

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17136982 332 KCHTIEEFrasNQRSAVLGNKIEMEITDLVEKNS-SLLRLGLHLEFNDARHRVAAHLQR 389
Cdd:COG5238 374 GNTTLREL---NLGKNNIGKQGAEALIDALQTNRlHTLILDGNLIGAEAQQRLEQLLER 429
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 251-368 3.65e-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: 45.55  E-value: 3.65e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 251 LIDLNLNNiKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQAL 330
Cdd:COG5238 322 LHTLNLAY-NGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDAL 400

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17136982 331 LkchtIEEFRASNQRSAVLGNKIEMEITDLVEKNSSLL 368
Cdd:COG5238 401 Q----TNRLHTLILDGNLIGAEAQQRLEQLLERIKSVY 434
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 242-390 3.40e-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: 42.47  E-value: 3.40e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 242 KRVKDDDSKLIDLNLNNIkniSDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPP 321
Cdd:COG5238 175 KALQNNSVETVYLGCNQI---GDEGIEELAEALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIGDE 251

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17136982 322 VIVKLVQALLKCHTIEEFRASnqrsavlGNKIEME----ITDLVEKNSSLlrLGLHLEFNDARHR----VAAHLQRN 390
Cdd:COG5238 252 GVIALAEALKNNTTVETLYLS-------GNQIGAEgaiaLAKALQGNTTL--TSLDLSVNRIGDEgaiaLAEGLQGN 319
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 261-377 3.84e-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: 42.47  E-value: 3.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 261 NISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFR 340
Cdd:COG5238 247 QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTLHTLN 326

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 17136982 341 -ASNQrsavLGNKIEMEITDLVEKNSSLLRlgLHLEFN 377
Cdd:COG5238 327 lAYNG----IGAQGAIALAKALQENTTLHS--LDLSDN 358
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 261-372 5.50e-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: 41.57  E-value: 5.50e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 261 NISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFr 340
Cdd:cd00116 148 RLEGASCEALAKALRANRDLKELNLANNGIGDAGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVL- 226

                        90       100       110
                ....*....|....*....|....*....|...
gi 17136982 341 asNQRSAVLGNKIEMEITD-LVEKNSSLLRLGL 372
Cdd:cd00116 227 --NLGDNNLTDAGAAALASaLLSPNISLLTLSL 257
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 261-372 6.61e-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: 41.70  E-value: 6.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17136982 261 NISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFR 340
Cdd:COG5238 219 PIGDEGAEILAEALKGNKSLTTLDLSNNQIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGAIALAKALQGNTTLTSLD 298

                        90       100       110
                ....*....|....*....|....*....|..
gi 17136982 341 ASNQRsavLGNKIEMEITDLVEKNSSLLRLGL 372
Cdd:COG5238 299 LSVNR---IGDEGAIALAEGLQGNKTLHTLNL 327
 
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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