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Conserved domains on  [gi|356519112|ref|XP_003528218|]
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exocyst complex component EXO70B1 isoform X1 [Glycine max]

Protein Classification

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. ...
371-678 2.59e-42

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: 157.44  E-value: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  371 RHAIKVMCVANRIVLPNERRLCEKVFEGFIHCEDLY-------PALRRIDVFQF---------WKNP-----VLPVIDAV 429
Cdd:pfam03081   1 SNWIQAYKIAVKGLFASERRLCDQVFSGSPSVRESCfaeiaqpSLDEFLQLLREfgeavasnlKRSPeklfkLLDMYEAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  430 R-LWESI-------GIQPPIYRINESR----------FDDLLYLTYSVKEQASVPSGRN-YRISIDVLDYIEIL--YQ-- 486
Cdd:pfam03081  81 SdLLPELeslfsgeACSELRSELAELLkrlgetaksiFSEFEEAIRRDSSKSPVPPDGGvHPLTRYVMNYLRKLaeYKdt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  487 -----------NWRGLFKTMLDKEGK-------LLYGHIAMITDLLDSSLEAISKNYNDPSLGYLFIINNRRFIEISAKR 548
Cdd:pfam03081 161 lsqllaslgdgGWLSSSSSPSLSSFDsgadgksLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIVQKVRR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  549 RGLSPIFGDDWLRKNTAKFQQNLELYQRSSWSKILNILKLDINESE-PNVAAK---LMKNKLCSFNEHLDDICNTQATWS 624
Cdd:pfam03081 241 SELGLLLGDDWLRRHEKKVKQYAKLYERESWGKVLSILLDEGLTSSsGGLSSKdkeQIKEKFKNFNEAFEELYRKQKSWV 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 356519112  625 VLNEELREQIIKSIENILLPAYGNFIARLQDFLGNHAfEYIEYGMFDIQDRLNN 678
Cdd:pfam03081 321 VPDPELREELRREISEKVVPAYRRFYDRYGDFLKNPE-KYVKYTPEDLENMLND 373
Cytochrome_b_N super family cl23723
Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit ...
47-176 7.15e-05

Cytochrome b (N-terminus)/b6/petB: Cytochrome b is a subunit of cytochrome bc1, an 11-subunit mitochondrial respiratory enzyme. Cytochrome b spans the mitochondrial membrane with 8 transmembrane helices (A-H) in eukaryotes. In plants and cyanobacteria, cytochrome b6 is analogous to eukaryote cytochrome b, containing two chains: helices A-D are encoded by the petB gene and helices E-H are encoded by the petD gene in these organisms. Cytochrome b/b6 contains two bound hemes and two ubiquinol/ubiquinone binding sites. The C-terminal portion of cytochrome b is described in a separate CD.


The actual alignment was detected with superfamily member cd08765:

Pssm-ID: 474033  Cd Length: 153  Bit Score: 43.73  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  47 KWTWWKILLYIGFSFIICLTVLFAKV---WECST----SPRVEAHMAFFILMITSVYAFFFDKEVKGKPDAYSLVSCAAF 119
Cdd:cd08765   11 EFNWHPVLMVIGFIFIQGIAIIVYRLpwtWKCSKllmkLIHAGLHILAFILAIISVVAVFVFHNAKNIPNMYSLHSWVGL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356519112 120 AIMSLALTRLShFGFEVDLLHFFSGVLTIQLMKIKLW--LVIVGGSFSYSLIILRSSLV 176
Cdd:cd08765   91 AAVILYPLQLV-LGISVYLLPVAPVRLRAALMPLHVYsgLFIFGTVIATALMGITEKLI 148
 
Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
371-678 2.59e-42

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: 157.44  E-value: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  371 RHAIKVMCVANRIVLPNERRLCEKVFEGFIHCEDLY-------PALRRIDVFQF---------WKNP-----VLPVIDAV 429
Cdd:pfam03081   1 SNWIQAYKIAVKGLFASERRLCDQVFSGSPSVRESCfaeiaqpSLDEFLQLLREfgeavasnlKRSPeklfkLLDMYEAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  430 R-LWESI-------GIQPPIYRINESR----------FDDLLYLTYSVKEQASVPSGRN-YRISIDVLDYIEIL--YQ-- 486
Cdd:pfam03081  81 SdLLPELeslfsgeACSELRSELAELLkrlgetaksiFSEFEEAIRRDSSKSPVPPDGGvHPLTRYVMNYLRKLaeYKdt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  487 -----------NWRGLFKTMLDKEGK-------LLYGHIAMITDLLDSSLEAISKNYNDPSLGYLFIINNRRFIEISAKR 548
Cdd:pfam03081 161 lsqllaslgdgGWLSSSSSPSLSSFDsgadgksLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIVQKVRR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  549 RGLSPIFGDDWLRKNTAKFQQNLELYQRSSWSKILNILKLDINESE-PNVAAK---LMKNKLCSFNEHLDDICNTQATWS 624
Cdd:pfam03081 241 SELGLLLGDDWLRRHEKKVKQYAKLYERESWGKVLSILLDEGLTSSsGGLSSKdkeQIKEKFKNFNEAFEELYRKQKSWV 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 356519112  625 VLNEELREQIIKSIENILLPAYGNFIARLQDFLGNHAfEYIEYGMFDIQDRLNN 678
Cdd:pfam03081 321 VPDPELREELRREISEKVVPAYRRFYDRYGDFLKNPE-KYVKYTPEDLENMLND 373
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
47-176 7.15e-05

Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate reductase 3, a cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. This protein is expressed at the brush border of duodenal enterocytes and may play a role in the uptake of dietary Fe(3+), facilitating its transport into the mucosal cells. It may also be involved in the recycling of extracellular ascorbate in erythrocyte membranes, and act as a ferrireductase in epithelial cells of the respiratory system. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176495  Cd Length: 153  Bit Score: 43.73  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  47 KWTWWKILLYIGFSFIICLTVLFAKV---WECST----SPRVEAHMAFFILMITSVYAFFFDKEVKGKPDAYSLVSCAAF 119
Cdd:cd08765   11 EFNWHPVLMVIGFIFIQGIAIIVYRLpwtWKCSKllmkLIHAGLHILAFILAIISVVAVFVFHNAKNIPNMYSLHSWVGL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356519112 120 AIMSLALTRLShFGFEVDLLHFFSGVLTIQLMKIKLW--LVIVGGSFSYSLIILRSSLV 176
Cdd:cd08765   91 AAVILYPLQLV-LGISVYLLPVAPVRLRAALMPLHVYsgLFIFGTVIATALMGITEKLI 148
 
Name Accession Description Interval E-value
Exo70 pfam03081
Exo70 exocyst complex subunit; The Exo70 protein forms one subunit of the exocyst complex. ...
371-678 2.59e-42

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: 157.44  E-value: 2.59e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  371 RHAIKVMCVANRIVLPNERRLCEKVFEGFIHCEDLY-------PALRRIDVFQF---------WKNP-----VLPVIDAV 429
Cdd:pfam03081   1 SNWIQAYKIAVKGLFASERRLCDQVFSGSPSVRESCfaeiaqpSLDEFLQLLREfgeavasnlKRSPeklfkLLDMYEAL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  430 R-LWESI-------GIQPPIYRINESR----------FDDLLYLTYSVKEQASVPSGRN-YRISIDVLDYIEIL--YQ-- 486
Cdd:pfam03081  81 SdLLPELeslfsgeACSELRSELAELLkrlgetaksiFSEFEEAIRRDSSKSPVPPDGGvHPLTRYVMNYLRKLaeYKdt 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  487 -----------NWRGLFKTMLDKEGK-------LLYGHIAMITDLLDSSLEAISKNYNDPSLGYLFIINNRRFIEISAKR 548
Cdd:pfam03081 161 lsqllaslgdgGWLSSSSSPSLSSFDsgadgksLLAHYIADIIDALLSNLEAKSKLYKDKALSGIFLMNNLHYIVQKVRR 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  549 RGLSPIFGDDWLRKNTAKFQQNLELYQRSSWSKILNILKLDINESE-PNVAAK---LMKNKLCSFNEHLDDICNTQATWS 624
Cdd:pfam03081 241 SELGLLLGDDWLRRHEKKVKQYAKLYERESWGKVLSILLDEGLTSSsGGLSSKdkeQIKEKFKNFNEAFEELYRKQKSWV 320
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 356519112  625 VLNEELREQIIKSIENILLPAYGNFIARLQDFLGNHAfEYIEYGMFDIQDRLNN 678
Cdd:pfam03081 321 VPDPELREELRREISEKVVPAYRRFYDRYGDFLKNPE-KYVKYTPEDLENMLND 373
Cyt_b561_CYBRD1 cd08765
Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate ...
47-176 7.15e-05

Vertebrate cytochrome b(561), CYBRD1 gene product; Duodenal cytochrome b or ferric-chelate reductase 3, a cytochrome b(561), as found in vertebrates, which might act as a ferric-chelate reductase, catalyzing the reduction of Fe(3+) to Fe(2+), such as associated with the transport of iron from the endosome to the cytoplasm. It is assumed that this protein uses ascorbate as the electron donor. This protein is expressed at the brush border of duodenal enterocytes and may play a role in the uptake of dietary Fe(3+), facilitating its transport into the mucosal cells. It may also be involved in the recycling of extracellular ascorbate in erythrocyte membranes, and act as a ferrireductase in epithelial cells of the respiratory system. Belongs to the cytochrome b(561) family, which are secretory vesicle-specific electron transport proteins. Cytochromes b(561) are integral membrane proteins that bind two heme groups non-covalently, and may have six alpha-helical trans-membrane segments.


Pssm-ID: 176495  Cd Length: 153  Bit Score: 43.73  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 356519112  47 KWTWWKILLYIGFSFIICLTVLFAKV---WECST----SPRVEAHMAFFILMITSVYAFFFDKEVKGKPDAYSLVSCAAF 119
Cdd:cd08765   11 EFNWHPVLMVIGFIFIQGIAIIVYRLpwtWKCSKllmkLIHAGLHILAFILAIISVVAVFVFHNAKNIPNMYSLHSWVGL 90
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 356519112 120 AIMSLALTRLShFGFEVDLLHFFSGVLTIQLMKIKLW--LVIVGGSFSYSLIILRSSLV 176
Cdd:cd08765   91 AAVILYPLQLV-LGISVYLLPVAPVRLRAALMPLHVYsgLFIFGTVIATALMGITEKLI 148
 
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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