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Conserved domains on  [gi|682358578|gb|KFY47586|]
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hypothetical protein V496_10558 [Pseudogymnoascus sp. VKM F-4515 (FW-2607)]

Protein Classification

AFI1/MesA family protein( domain architecture ID 10544612)

AFI1/MesA family protein similar to Aspergillus nidulans protein mesA that is required for the formation of actin cables at hyphal tips

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
 436-547 2.21e-54

Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque of the spindle pole body. In Aspergillus nidulans the protein member is necessary for stabilization of the polarity axes during septation. and in S. cerevisiae it functions as a polarization-specific docking factor.


:

Pssm-ID: 400783  Cd Length: 113  Bit Score: 183.26  E-value: 2.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682358578  436 LHSHLTTGGAYTHPIIVLVNAILTQKRVIFLGHNRPSGEVAEAVLAACALASGG-ILRGFTRHAFPYTDLSKIDDLLKVP 514
Cdd:pfam08616   1 NHSLLKLLGPFTPPIILLINALLTSKRIIFLSYQRSAGEVSEFVLALCNLISGGfVLRGFTNNSFPYVDLSKLDALRKVP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 682358578  515 GFIAGVTNPTFENHPEWWDVLCDLPTGRMKISA 547
Cdd:pfam08616  81 GYIAGVTNPIFENQDQWWDVLCDLDSGSVKLSK 113
Afi1 pfam07792
Docking domain of Afi1 for Arf3 in vesicle trafficking; This domain occurs at the N-terminal ...
 118-249 3.69e-42

Docking domain of Afi1 for Arf3 in vesicle trafficking; This domain occurs at the N-terminal of Afi1, an Arf3p-interacting protein, is a protein necessary for vesicle trafficking in yeast. This domain is the interacting region of the protein which binds to Arf3, the highly conserved small GTPases (ADP-ribosylation factors). Afi1 is distributed asymmetrically at the plasma membrane and is required for polarized distribution of Arf3 but not of an Arf3 guanine nucleotide-exchange factor, Yel1p. However, Afi1 is not required for targeting of Arf3 or Yel1p to the plasma membrane. Afi1 functions as an Arf3 polarization-specific adapter and participates in development of polarity. Although Arf3 is the homolog of human Arf6 it does not function in the same way, not being necessary for endocytosis or for mating factor receptor internalization. In the S phase, however, it is concentrated at the plasma membrane of the emerging bud. Because of its polarized localization and its critical function in the normal budding pattern of yeast, Arf3 is probably a regulator of vesicle trafficking, which is important for polarized growth.


:

Pssm-ID: 400236  Cd Length: 119  Bit Score: 149.53  E-value: 3.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682358578  118 YILVASFDIDRGPVMEHQYPVAITGDEHM--LAELMLPDQAHVRNQDWTIFFLHKDTSQEEEEAELKAEKRRRKKRRKDi 195
Cdd:pfam07792   1 YILVAEFDIDKGPVVKHQYPSAIPGDEGMqnLAELMLPDQVHKRPQDWTVFFLYKDTSTEEYELFNNKLKYRRKSKSHD- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 682358578  196 aEGLVEADQVDEADFENHPsdddsnsseesedeGGEGPPLIYVLNLVNTKQDKT 249
Cdd:pfam07792  80 -DDILEEDEEDESSDEEEI--------------GGEGPPLLYVLNVVNTKQDKS 118
 
Name Accession Description Interval E-value
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
 436-547 2.21e-54

Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque of the spindle pole body. In Aspergillus nidulans the protein member is necessary for stabilization of the polarity axes during septation. and in S. cerevisiae it functions as a polarization-specific docking factor.


Pssm-ID: 400783  Cd Length: 113  Bit Score: 183.26  E-value: 2.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682358578  436 LHSHLTTGGAYTHPIIVLVNAILTQKRVIFLGHNRPSGEVAEAVLAACALASGG-ILRGFTRHAFPYTDLSKIDDLLKVP 514
Cdd:pfam08616   1 NHSLLKLLGPFTPPIILLINALLTSKRIIFLSYQRSAGEVSEFVLALCNLISGGfVLRGFTNNSFPYVDLSKLDALRKVP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 682358578  515 GFIAGVTNPTFENHPEWWDVLCDLPTGRMKISA 547
Cdd:pfam08616  81 GYIAGVTNPIFENQDQWWDVLCDLDSGSVKLSK 113
Afi1 pfam07792
Docking domain of Afi1 for Arf3 in vesicle trafficking; This domain occurs at the N-terminal ...
 118-249 3.69e-42

Docking domain of Afi1 for Arf3 in vesicle trafficking; This domain occurs at the N-terminal of Afi1, an Arf3p-interacting protein, is a protein necessary for vesicle trafficking in yeast. This domain is the interacting region of the protein which binds to Arf3, the highly conserved small GTPases (ADP-ribosylation factors). Afi1 is distributed asymmetrically at the plasma membrane and is required for polarized distribution of Arf3 but not of an Arf3 guanine nucleotide-exchange factor, Yel1p. However, Afi1 is not required for targeting of Arf3 or Yel1p to the plasma membrane. Afi1 functions as an Arf3 polarization-specific adapter and participates in development of polarity. Although Arf3 is the homolog of human Arf6 it does not function in the same way, not being necessary for endocytosis or for mating factor receptor internalization. In the S phase, however, it is concentrated at the plasma membrane of the emerging bud. Because of its polarized localization and its critical function in the normal budding pattern of yeast, Arf3 is probably a regulator of vesicle trafficking, which is important for polarized growth.


Pssm-ID: 400236  Cd Length: 119  Bit Score: 149.53  E-value: 3.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682358578  118 YILVASFDIDRGPVMEHQYPVAITGDEHM--LAELMLPDQAHVRNQDWTIFFLHKDTSQEEEEAELKAEKRRRKKRRKDi 195
Cdd:pfam07792   1 YILVAEFDIDKGPVVKHQYPSAIPGDEGMqnLAELMLPDQVHKRPQDWTVFFLYKDTSTEEYELFNNKLKYRRKSKSHD- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 682358578  196 aEGLVEADQVDEADFENHPsdddsnsseesedeGGEGPPLIYVLNLVNTKQDKT 249
Cdd:pfam07792  80 -DDILEEDEEDESSDEEEI--------------GGEGPPLLYVLNVVNTKQDKS 118
 
Name Accession Description Interval E-value
SPA pfam08616
Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque ...
 436-547 2.21e-54

Stabilization of polarity axis; Swiss:Q99222 has been shown to interact with the outer plaque of the spindle pole body. In Aspergillus nidulans the protein member is necessary for stabilization of the polarity axes during septation. and in S. cerevisiae it functions as a polarization-specific docking factor.


Pssm-ID: 400783  Cd Length: 113  Bit Score: 183.26  E-value: 2.21e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682358578  436 LHSHLTTGGAYTHPIIVLVNAILTQKRVIFLGHNRPSGEVAEAVLAACALASGG-ILRGFTRHAFPYTDLSKIDDLLKVP 514
Cdd:pfam08616   1 NHSLLKLLGPFTPPIILLINALLTSKRIIFLSYQRSAGEVSEFVLALCNLISGGfVLRGFTNNSFPYVDLSKLDALRKVP 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 682358578  515 GFIAGVTNPTFENHPEWWDVLCDLPTGRMKISA 547
Cdd:pfam08616  81 GYIAGVTNPIFENQDQWWDVLCDLDSGSVKLSK 113
Afi1 pfam07792
Docking domain of Afi1 for Arf3 in vesicle trafficking; This domain occurs at the N-terminal ...
 118-249 3.69e-42

Docking domain of Afi1 for Arf3 in vesicle trafficking; This domain occurs at the N-terminal of Afi1, an Arf3p-interacting protein, is a protein necessary for vesicle trafficking in yeast. This domain is the interacting region of the protein which binds to Arf3, the highly conserved small GTPases (ADP-ribosylation factors). Afi1 is distributed asymmetrically at the plasma membrane and is required for polarized distribution of Arf3 but not of an Arf3 guanine nucleotide-exchange factor, Yel1p. However, Afi1 is not required for targeting of Arf3 or Yel1p to the plasma membrane. Afi1 functions as an Arf3 polarization-specific adapter and participates in development of polarity. Although Arf3 is the homolog of human Arf6 it does not function in the same way, not being necessary for endocytosis or for mating factor receptor internalization. In the S phase, however, it is concentrated at the plasma membrane of the emerging bud. Because of its polarized localization and its critical function in the normal budding pattern of yeast, Arf3 is probably a regulator of vesicle trafficking, which is important for polarized growth.


Pssm-ID: 400236  Cd Length: 119  Bit Score: 149.53  E-value: 3.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 682358578  118 YILVASFDIDRGPVMEHQYPVAITGDEHM--LAELMLPDQAHVRNQDWTIFFLHKDTSQEEEEAELKAEKRRRKKRRKDi 195
Cdd:pfam07792   1 YILVAEFDIDKGPVVKHQYPSAIPGDEGMqnLAELMLPDQVHKRPQDWTVFFLYKDTSTEEYELFNNKLKYRRKSKSHD- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 682358578  196 aEGLVEADQVDEADFENHPsdddsnsseesedeGGEGPPLIYVLNLVNTKQDKT 249
Cdd:pfam07792  80 -DDILEEDEEDESSDEEEI--------------GGEGPPLLYVLNVVNTKQDKS 118
 
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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