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Conserved domains on  [gi|247269408|ref|NP_058553|]
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exocyst complex component 7 isoform 1 [Mus musculus]

Protein Classification

EXO70 family protein( domain architecture ID 10503717)

EXO70 family protein similar to Saccharomyces cerevisiae exocyst complex component EXO70 and Homo sapiens exocyst complex component 7

CATH:  1.20.1280.170
PubMed:  16249794
SCOP:  4001555

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
313-691 1.98e-83

Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. First discovered in S. cerevisiae, Exo70 and other exocyst proteins have been observed in several other eukaryotes, including humans. In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localized at the tip of the bud, the major site of exocytosis in yeast. Exo70 interacts with the Rho3 GTPase. This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud). In humans, the functions of Exo70 and the exocyst complex are less well characterized: Exo70 is expressed in several tissues and is thought to also be involved in exocytosis.


:

Pssm-ID: 460798  Cd Length: 373  Bit Score: 268.37  E-value: 1.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  313 YIHCVSAFVKLAQSEYRLLMEIIPE--HHQKKTFDSLIQDALDGLMLEGENIVSAARKAIIR--HDFSTVLTVFPILRHL 388
Cdd:pfam03081   4 IQAYKIAVKGLFASERRLCDQVFSGspSVRESCFAEIAQPSLDEFLQLLREFGEAVASNLKRspEKLFKLLDMYEALSDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  389 KqtkPEFDQVLQGTAAST-KNKLPGLITSMETIGAKALEDFADNIKNDPDKEyNMPKDGTVHELTSNAILFLQQLLDFQE 467
Cdd:pfam03081  84 L---PELESLFSGEACSElRSELAELLKRLGETAKSIFSEFEEAIRRDSSKS-PVPPDGGVHPLTRYVMNYLRKLAEYKD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  468 TAGAMLASQVLGDtyniPLDPRETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYIL 547
Cdd:pfam03081 160 TLSQLLASLGDGG----WLSSSSSPSLSSFDSGADGKSLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  548 KSLEKSELIQLVavtQKTAERSYREHIEQQIQTYQR-SWLKVTDYIAEKNLPVFqpGVKLRDKERQMIKERFKGFNDGLE 626
Cdd:pfam03081 236 QKVRRSELGLLL---GDDWLRRHEKKVKQYAKLYEReSWGKVLSILLDEGLTSS--SGGLSSKDKEQIKEKFKNFNEAFE 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 247269408  627 ELCKIQKVWAIPDTEQRDKIRQAQKDIVKETYGAFLHRYGsvPFTKNPEKYIKYRVEQVGDMIDR 691
Cdd:pfam03081 311 ELYRKQKSWVVPDPELREELRREISEKVVPAYRRFYDRYG--DFLKNPEKYVKYTPEDLENMLND 373
 
Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
313-691 1.98e-83

Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. First discovered in S. cerevisiae, Exo70 and other exocyst proteins have been observed in several other eukaryotes, including humans. In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localized at the tip of the bud, the major site of exocytosis in yeast. Exo70 interacts with the Rho3 GTPase. This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud). In humans, the functions of Exo70 and the exocyst complex are less well characterized: Exo70 is expressed in several tissues and is thought to also be involved in exocytosis.


Pssm-ID: 460798  Cd Length: 373  Bit Score: 268.37  E-value: 1.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  313 YIHCVSAFVKLAQSEYRLLMEIIPE--HHQKKTFDSLIQDALDGLMLEGENIVSAARKAIIR--HDFSTVLTVFPILRHL 388
Cdd:pfam03081   4 IQAYKIAVKGLFASERRLCDQVFSGspSVRESCFAEIAQPSLDEFLQLLREFGEAVASNLKRspEKLFKLLDMYEALSDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  389 KqtkPEFDQVLQGTAAST-KNKLPGLITSMETIGAKALEDFADNIKNDPDKEyNMPKDGTVHELTSNAILFLQQLLDFQE 467
Cdd:pfam03081  84 L---PELESLFSGEACSElRSELAELLKRLGETAKSIFSEFEEAIRRDSSKS-PVPPDGGVHPLTRYVMNYLRKLAEYKD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  468 TAGAMLASQVLGDtyniPLDPRETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYIL 547
Cdd:pfam03081 160 TLSQLLASLGDGG----WLSSSSSPSLSSFDSGADGKSLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  548 KSLEKSELIQLVavtQKTAERSYREHIEQQIQTYQR-SWLKVTDYIAEKNLPVFqpGVKLRDKERQMIKERFKGFNDGLE 626
Cdd:pfam03081 236 QKVRRSELGLLL---GDDWLRRHEKKVKQYAKLYEReSWGKVLSILLDEGLTSS--SGGLSSKDKEQIKEKFKNFNEAFE 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 247269408  627 ELCKIQKVWAIPDTEQRDKIRQAQKDIVKETYGAFLHRYGsvPFTKNPEKYIKYRVEQVGDMIDR 691
Cdd:pfam03081 311 ELYRKQKSWVVPDPELREELRREISEKVVPAYRRFYDRYG--DFLKNPEKYVKYTPEDLENMLND 373
 
Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
313-691 1.98e-83

Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. First discovered in S. cerevisiae, Exo70 and other exocyst proteins have been observed in several other eukaryotes, including humans. In S. cerevisiae, the exocyst complex is involved in the late stages of exocytosis, and is localized at the tip of the bud, the major site of exocytosis in yeast. Exo70 interacts with the Rho3 GTPase. This interaction mediates one of the three known functions of Rho3 in cell polarity: vesicle docking and fusion with the plasma membrane (the other two functions are regulation of actin polarity and transport of exocytic vesicles from the mother cell to the bud). In humans, the functions of Exo70 and the exocyst complex are less well characterized: Exo70 is expressed in several tissues and is thought to also be involved in exocytosis.


Pssm-ID: 460798  Cd Length: 373  Bit Score: 268.37  E-value: 1.98e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  313 YIHCVSAFVKLAQSEYRLLMEIIPE--HHQKKTFDSLIQDALDGLMLEGENIVSAARKAIIR--HDFSTVLTVFPILRHL 388
Cdd:pfam03081   4 IQAYKIAVKGLFASERRLCDQVFSGspSVRESCFAEIAQPSLDEFLQLLREFGEAVASNLKRspEKLFKLLDMYEALSDL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  389 KqtkPEFDQVLQGTAAST-KNKLPGLITSMETIGAKALEDFADNIKNDPDKEyNMPKDGTVHELTSNAILFLQQLLDFQE 467
Cdd:pfam03081  84 L---PELESLFSGEACSElRSELAELLKRLGETAKSIFSEFEEAIRRDSSKS-PVPPDGGVHPLTRYVMNYLRKLAEYKD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  468 TAGAMLASQVLGDtyniPLDPRETSSSATSYSSEFSKRLLSTYICKVLGNLQLNLLSKSKVYEDPALSAIFLHNNYNYIL 547
Cdd:pfam03081 160 TLSQLLASLGDGG----WLSSSSSPSLSSFDSGADGKSLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 247269408  548 KSLEKSELIQLVavtQKTAERSYREHIEQQIQTYQR-SWLKVTDYIAEKNLPVFqpGVKLRDKERQMIKERFKGFNDGLE 626
Cdd:pfam03081 236 QKVRRSELGLLL---GDDWLRRHEKKVKQYAKLYEReSWGKVLSILLDEGLTSS--SGGLSSKDKEQIKEKFKNFNEAFE 310
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 247269408  627 ELCKIQKVWAIPDTEQRDKIRQAQKDIVKETYGAFLHRYGsvPFTKNPEKYIKYRVEQVGDMIDR 691
Cdd:pfam03081 311 ELYRKQKSWVVPDPELREELRREISEKVVPAYRRFYDRYG--DFLKNPEKYVKYTPEDLENMLND 373
 
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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