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Conserved domains on  [gi|145359159|ref|NP_200048|]
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exocyst subunit exo70 family protein A3 [Arabidopsis thaliana]

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. ...
223-573 2.76e-125

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: 373.15  E-value: 2.76e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  223 NWIHYIRISVKLLFAAEKEICHQILDGVEPFRDQSFAEITTISFGMLL----SFGYAIA-ISRRSPEKVFVILDMYEIMI 297
Cdd:pfam03081   2 NWIQAYKIAVKGLFASERRLCDQVFSGSPSVRESCFAEIAQPSLDEFLqllrEFGEAVAsNLKRSPEKLFKLLDMYEALS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  298 ELQPEFELIFGSKPCTEMKEDALNLTKLLAQTVKETIADFEVAIEMDATETVVM-DGSVHALTSYVARYVKFLFDYEPTL 376
Cdd:pfam03081  82 DLLPELESLFSGEACSELRSELAELLKRLGETAKSIFSEFEEAIRRDSSKSPVPpDGGVHPLTRYVMNYLRKLAEYKDTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  377 RQLFQEF------------------NSNDPDTKLKSVMTGIMRALRNNLDGKSRQFEDAALTQLFLMNNVYYIVRNFRRE 438
Cdd:pfam03081 162 SQLLASLgdggwlssssspslssfdSGADGKSLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIVQKVRRS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  439 EAKNFLGDDLVQTHRRIVQQHAKQYQTISWNKILQCITVQSSKSGLIKNESIKKTLVKEKFKTFNSQFEELHQRQCQWSV 518
Cdd:pfam03081 242 ELGLLLGDDWLRRHEKKVKQYAKLYERESWGKVLSILLDEGLTSSSGGLSSKDKEQIKEKFKNFNEAFEELYRKQKSWVV 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145359159  519 SDVELRESLRLAIAEVLLPAYGSFLKRFGPMIesgKNSQKYIRFTPEDLERMLND 573
Cdd:pfam03081 322 PDPELREELRREISEKVVPAYRRFYDRYGDFL---KNPEKYVKYTPEDLENMLND 373
 
Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
223-573 2.76e-125

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: 373.15  E-value: 2.76e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  223 NWIHYIRISVKLLFAAEKEICHQILDGVEPFRDQSFAEITTISFGMLL----SFGYAIA-ISRRSPEKVFVILDMYEIMI 297
Cdd:pfam03081   2 NWIQAYKIAVKGLFASERRLCDQVFSGSPSVRESCFAEIAQPSLDEFLqllrEFGEAVAsNLKRSPEKLFKLLDMYEALS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  298 ELQPEFELIFGSKPCTEMKEDALNLTKLLAQTVKETIADFEVAIEMDATETVVM-DGSVHALTSYVARYVKFLFDYEPTL 376
Cdd:pfam03081  82 DLLPELESLFSGEACSELRSELAELLKRLGETAKSIFSEFEEAIRRDSSKSPVPpDGGVHPLTRYVMNYLRKLAEYKDTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  377 RQLFQEF------------------NSNDPDTKLKSVMTGIMRALRNNLDGKSRQFEDAALTQLFLMNNVYYIVRNFRRE 438
Cdd:pfam03081 162 SQLLASLgdggwlssssspslssfdSGADGKSLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIVQKVRRS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  439 EAKNFLGDDLVQTHRRIVQQHAKQYQTISWNKILQCITVQSSKSGLIKNESIKKTLVKEKFKTFNSQFEELHQRQCQWSV 518
Cdd:pfam03081 242 ELGLLLGDDWLRRHEKKVKQYAKLYERESWGKVLSILLDEGLTSSSGGLSSKDKEQIKEKFKNFNEAFEELYRKQKSWVV 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145359159  519 SDVELRESLRLAIAEVLLPAYGSFLKRFGPMIesgKNSQKYIRFTPEDLERMLND 573
Cdd:pfam03081 322 PDPELREELRREISEKVVPAYRRFYDRYGDFL---KNPEKYVKYTPEDLENMLND 373
 
Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
223-573 2.76e-125

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: 373.15  E-value: 2.76e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  223 NWIHYIRISVKLLFAAEKEICHQILDGVEPFRDQSFAEITTISFGMLL----SFGYAIA-ISRRSPEKVFVILDMYEIMI 297
Cdd:pfam03081   2 NWIQAYKIAVKGLFASERRLCDQVFSGSPSVRESCFAEIAQPSLDEFLqllrEFGEAVAsNLKRSPEKLFKLLDMYEALS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  298 ELQPEFELIFGSKPCTEMKEDALNLTKLLAQTVKETIADFEVAIEMDATETVVM-DGSVHALTSYVARYVKFLFDYEPTL 376
Cdd:pfam03081  82 DLLPELESLFSGEACSELRSELAELLKRLGETAKSIFSEFEEAIRRDSSKSPVPpDGGVHPLTRYVMNYLRKLAEYKDTL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  377 RQLFQEF------------------NSNDPDTKLKSVMTGIMRALRNNLDGKSRQFEDAALTQLFLMNNVYYIVRNFRRE 438
Cdd:pfam03081 162 SQLLASLgdggwlssssspslssfdSGADGKSLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIVQKVRRS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145359159  439 EAKNFLGDDLVQTHRRIVQQHAKQYQTISWNKILQCITVQSSKSGLIKNESIKKTLVKEKFKTFNSQFEELHQRQCQWSV 518
Cdd:pfam03081 242 ELGLLLGDDWLRRHEKKVKQYAKLYERESWGKVLSILLDEGLTSSSGGLSSKDKEQIKEKFKNFNEAFEELYRKQKSWVV 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145359159  519 SDVELRESLRLAIAEVLLPAYGSFLKRFGPMIesgKNSQKYIRFTPEDLERMLND 573
Cdd:pfam03081 322 PDPELREELRREISEKVVPAYRRFYDRYGDFL---KNPEKYVKYTPEDLENMLND 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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